| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.84805023 |
| Since an EF Tu dependent fluorescence change was also observed with fluorescein labeled tRNA ( Phe ) , the protein dependent structural change is effected by direct interactions between EF Tu and the tRNA and does not require the aminoacyl group . 0.84805023^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.84544923 |
| The results indicate that , on the ribosome , EF Tu interacts with peptidyl site bound peptidyl tRNA through tRNA binding site 2 and with aminoacyl site bound aminoacyl tRNA through tRNA binding site I . . 0.84544923^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.76532656 |
| Our results unequivocally show that different regions of the aa tRNA are needed for a coordinated interaction with EF Tu . . 0.76532656^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.56151369 |
| The elongation factor Tu binds aminoacyl tRNA in the presence of GDP . 0.56151369^^^ Escherichia coli elongation factor ( EF Tu ) binds aminoacyl tRNAs ( aa tRNA ) not only in the presence of GTP but also in the presence of GDP . 0.51057569^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.74919785 |
| Interaction of aminoacyl tRNA with bacterial elongation factor Tu : GTP complex : effects of the amino group of amino acid esterified to tRNA , the amino acid side chain , and tRNA structure . 0.74919785^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.50614266 |
| Kinetic analysis indicated that EF 1 alpha formed a complex with the hDRS Asp tRNA complex and stimulated the dissociation of Asp tRNA . 0.50614266^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.63718911 |
| Thus , although the interactions between elongation factor Tu and tRNA accelerate the rate of NH proton exchange in the aminoacyl stem region , the Phe tRNA ( Phe ) preserves its typical L shaped tertiary structure in the complex . 0.63718911^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.5424366 |
| Part of the structure of translational elongation factor G , in a complex with GDP , resembles the tRNA bound in a ternary complex with elongation factor Tu and GTP ; this ' molecular mimicry ' extends to charge distribution as well as shape . . 0.5424366^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.702203 |
| The translation elongation factor EF Tu in its GTP bound state forms a ternary complex with any aminoacylated tRNA ( aa tRNA ) , except initiator tRNA and selenocysteinyl tRNA . 0.702203^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.88020504 |
| Surprisingly , the interaction between eEF1A and Exp 5 is dependent on tRNA that can interact directly with Exp 5 and , if aminoacylated , recruits eEF1A into the export complex . 0.88020504^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.7052645 |
| The tRNA anticodon stem is bent sharply toward the enzyme as compared with its conformation when bound to elongation factor Tu , providing an essential basis for shape selective recognition . 0.7052645^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.70832172 |
| In the other conformation , presumptive aminoacylated tRNA is bound only by the anticodon , the acceptor stem being free and having space to interact precisely with EF 1alpha , suggesting that the product of aminoacylation can be directly handed off to EF 1alpha for the next step of protein synthesis . . 0.70832172^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The modified tRNA is fully active in the aminoacylation assay ; when aminoacylated it is recognized by the elongation factor Tu ( EF Tu ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| These aminoacyl oligonucleotides inhibit both the formation of ternary complex EF Tu GTP AA tRNA and the interaction of this complex with the ribosomal A site . ^^^ The uncoupled EF Tu dependent GTPase ( in the absence of AA tRNA ) was also inhibited by C A Phe , C A ( 2 ' Phe ) H , and C A ( 2 ' H ) Phe , while nonenzymatic binding of Phe tRNA to the ribosomal A site was inhibited by C A Phe and C A ( 2 ' Phe ) H , but not by C A ( 2 ' H ) Phe . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Editing mechanisms in aminoacylation of tRNA : ATP consumption and the binding of aminoacyl tRNA by elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| That the resulting `` chemically aminoacylated ' ' tRNA ' s were identical with those prepared by enzymatic aminoacylation was judged by comparison of 1 ) chromatographic properties on benzolated diethylaminoethyl cellulose , 2 ) rates of chemical deacylation , and 3 ) affinities for elongation factor Tu , as well as 4 ) the ability of misacylated tRNA ' s so derived to be deacylated chemically and then reactivated enzymatically with their cognate amino acids . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Recent suggestions that elongation factor Tu ( EF Tu ) is specific for 2 ' O aminoacyl tRNA , as compared with the 3 ' isomer , prompted us to assay [ 3H ] aminoacyl tRNAs from Escherichia coli terminating in 2 ' or 3 ' deoxyadenosine for binding to EF Tu to determine the possible positional specificity of the factor . ^^^ Six modified tRNA isoacceptors ( including tRNATrp and tRNATyr , for which both modified aminoacyl tRNAs were accessible by enzymatic aminoacylation ) were used in gel filtration experiments to permit direct measurement of the individual aminoacyl tRNA EF Tu GTP complexes . ^^^ The results were completely consistent with those obtained by the deacylation procedure and indicated that EF Tu can bind to both positional isomers of aminoacyl tRNA with no obvious preference for either . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| It is concluded that 2 ' as well as 3 ' isomers of native aminoacyl tRNA can be utilized for ternary complex formation but in a following step a uniform 2 ' aminoacyl tRNA EF Tu GTP complex is formed . ^^^ Specificity of elongation factor Tu from Escherichia coli with respect to attachment to the amino acid to the 2 ' or 3 ' hydroxyl group of the terminal adenosine of tRNA . ^^^ Although the free vicinal hydroxyl group of the terminal adenosine is not absolutely required , replacement of the ester linkage through with the amino acid is attached to tRNA by an amide linkage leads to loss of ability to interact with elongation factor Tu . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A ternary complex of elongation factor Tu , GTP and the modified Arg tRNA , can be formed allowing future studies of enzymatic binding to the ribosome . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| They include a set of genes for rRNA ' s ( rrnB ) , a gene for spacer tRNA , tRNA2Glu ( tgtB ) , one of the two genes for EF Tu ( tufB ) , genes for four ribosomal proteins ( rplK , A , J , and L ) , genes for the beta and beta ' subunits of RNA polymerase ( rpoB and rpoC ) , and genes for three tRNA ' s ( tyrU , gluT , and thrT ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Both positional isomers of aminoacyl tRNA ' s are bound by elongation factor Tu . ^^^ Six purified Escherichia coli and yeast tRNA ' s were converted to positionally defined tRNA ' s terminating in 2 ' and 3 ' deoxyadenosine ; the modified ( amino acyl ) tRNA ' s were compared for their abilities to bind to elongation factor Tu ( EF Tu ) in the presence both of GTP and guanylylimidodiphosphate ( GMP P ( NH ) P ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| C G A A ( 14 pmol ) was bound to tRNAPhe in the complete system containing elongation factor Tu GTP Phe tRNA ( uridylyl 3 ' , 5 ' ) 7 uridine 30S ribosomes ( 100 pmol ) . ^^^ In the `` nonenzymatic ' ' binding ( i . e . , no elongation factor Tu GTP ) of Phe tRNA a sigmoidal Mg2+ dependence was found , whereas the `` enzymatic ' ' binding ( elongation factor Tu GTP present ) showed a hyperbolic curve . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| DNA directed in vitro synthesis of beta galactosidase : dependencies on elongation factor Tu and tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The mechanism of the interaction of uncharged tRNA and stringent factor with the ribosomes during the in vitro synthesis of guanosine polypnophates ( pppGpp and ppGpp ) was studied . 70S ribosomes lacking proteins L 7 and L 12 were able to bind radioactive stringent factor but not EF Tu or EF G . ^^^ In addition , ribosomes carrying EF Tu , GMPPCP and Phe tRNA bound as much stringent factor as 70S ribosomes alone . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Dissociation of aminoacyl tRNA from the complex of EF Tu GTP aminoacyl tRNA by extracts of Escherichia coli . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A similar change in the spectrum was also observed when aminoacyl tRNA , but not deacylated tRNA , was added to EF Tu GDP ANS complex . ^^^ These results suggest that in EF Tu GTP the conformation was altered and one additional binding site for ANS was created at or near the site interacting with aminoacyl tRNA . ^^^ Another reagent , N ( 1 anilinonaphthyl 4 ) maleimide ( ANM ) was covalently bound to the sulfhydryl group in EF Tu GDP which is essential for interaction with aminoacyl tRNA . ^^^ The difference in the reactivity of the sulfhydryl group essential for aminoacyl tRNA binding between EF Tu GTP and EF Tu GDP probably reflects a conformational transition of the protein near the active site . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Nucleotide ( nt ) sequences encoding the elongation factor Tu ( EF Tu ) , tRNA ( Thr ) and tRNA ( Trp ) from Chlamydia trachomatis have been determined . ^^^ The environment of the EF Tu encoding gene ( tuf ) , between two tRNA gene sequences , suggests that it is part of a tufB locus . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The ability of the mixture of the 37+43 kDa fragments , including this amino terminal peptide 1 36 , to bind GDP or to facilitate aminoacyl tRNA binding to salt washed ribosomes was severely reduced , compared to intact EF 1 alpha . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Eukaryotic elongation factor 1 alpha ( EF 1 alpha ) binds all the aminoacyl tRNAs except the initiator tRNA in a GTP dependent manner . ^^^ In order to better understand this site , we have initiated cross linking and protease mapping studies of the EF 1 alpha GTP aminoacyl tRNA complex . ^^^ Two different chemical cross linking reagents , trans diaminedichloroplatinum ( 2 ) and diepoxybutane , were used to cross link four different aminoacyl tRNA species to EF 1 alpha . ^^^ Last , an aminoacyl tRNA analog with a reactive group on the aminoacyl side chain , N epsilon bromoacetyl Lys tRNA , was cross linked to EF 1 alpha . ^^^ A model is developed for aminoacyl tRNA binding to EF 1 alpha based on its similarity to the prokaryotic factor EF Tu , for which an 10 ray crystal structure is available . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The purified protein was identified with EF 1 alpha on criteria of molecular mass , cross reaction with antibodies raised against Artemia salina EF 1 alpha , affinity for guanine nucleotides , and ability to promote the mRNA dependent binding of aminoacyl tRNA to 80S ribosomes . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Our data indicate that ms2i6A has no effect on codon anticodon interactions on wild type ribosomes as long as aminoacyl tRNA is in ternary complex with EF Tu and GTP . ms2i6A deficiency in the cognate poly ( U ) reader tRNA ( Phe ) leads to increased misreading when the near cognate competitor tRNA 4 ( Leu ) is wild type . ms2i6A deficiency in tRNA 4 ( Leu ) gives a decreased error level in competition with wild type tRNA ( Phe ) . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Nonsense codon suppression by tyrT ( Su 3 ) suppressor tRNA was reduced by 2661C in a rpsL 224 strain in the presence of EF Tu ( As ) but not in the presence of EF Tu ( Aa ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Mutations in selC , which reduce the 8 base pair aminoacyl acceptor helix to the canonical 7 base pair length ( tRNA ( Sec ) ( delAc ] or which replace the extra arm of tRNA ( Sec ) by that of a serine acceptor tRNA species ( tRNA ( Sec ) ( ExS ) , block the function in selenoprotein synthesis in vivo ( Baron , C . , Heider , J . , and Bck , A . ( 1990 ) Nucleic Acids Res . 18 , 6761 6766 ) . tRNA ( Sec ) , tRNA ( Sec ) ( delAc ) , and tRNA ( Sec ) ( ExS ) were purified and analyzed for their interaction with purified seryl tRNA synthetase , selenocysteine synthase and translation factors SELB and EF Tu . ^^^ Reduction of the length of the aminoacyl acceptor stem to 7 base pairs prevented the interaction with translation factor SELB but allowed binding to EF Tu , irrespective of whether tRNA ( Sec ) ( delAc ) was charged with serine or selenocysteine . ^^^ The aminoacyl acceptor helix of tRNA ( Sec ) , therefore , is a major determinant directing binding to SELB and precluding interaction with EF Tu . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Intact , native EF Tu , isolated using previously described methods and fully active in binding GTP , was never found to be fully active in binding aminoacyl tRNA as judged by high performance liquid chromatography ( HPLC ) gel filtration and zone interference gel electrophoresis . ^^^ GTP and aminoacyl tRNA , free of deacylated tRNA and inactive EF Tu , has become possible using HPLC gel filtration . ^^^ Isolation and stability of ternary complexes of elongation factor Tu , GTP and aminoacyl tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Like EF 1 alpha , purified thesaurin a binds tRNA , GDP , and GTP . ^^^ Unlike EF 1 alpha , thesaurin a binds discharged tRNA more tightly than charged tRNA , and GTP more tightly than GDP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We have studied the interaction between EF Tu GDP or EF Tu GTP in complex with kirromycin or aurodox ( N 1 methylkirromycin ) and aminoacyl tRNA , N acetylaminoacyl tRNA , or deacylated tRNA . ^^^ All three methods revealed that kirromycin induces a severe drop in the stability of the complex of EF Tu GTP and aminoacyl tRNA of about 3 orders of magnitude . ^^^ The affinities of EF Tu kirromycin GTP and EF Tu kirromycin GDP for aa tRNA were found to be of about the same order of magnitude . ^^^ We conclude that kirromycin and related compounds do not induce a so called GTP like conformation of EF Tu with respect to tRNA binding . ^^^ A . 71 , 4910 4914 ] , we were unable to demonstrate complexes of EF Tu aurodox GTP / GDP with N acetylaminoacyl tRNA or deacylated tRNA by direct detection using zone interference gel electrophoresis . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| How many EF Tu molecules participate in aminoacyl tRNA binding and peptide bond formation in Escherichia coli translation . ^^^ We suggest , on the basis of these data , that aminoacyl tRNA enters the ribosomal A site in a pentameric complex together with two EF Tu and two GTP molecules . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The interaction of 18 different Escherichia coli aminoacyl tRNA species with elongation factor Tu and GTP has been measured by a fluorescence titration assay under equilibrium conditions . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In a poly ( U ) dependent system with high accuracy in poly ( Phe ) synthesis , the acceptance of the cognate ternary complex Phe tRNA EF Tu GTP ( which has the correct anticodon with respect to the codon at the A site ) was compared with the competing acceptance of ternary complexes with near cognate Leu tRNA ( Leu ) ( which has a similar anticodon ) or non cognate Asp tRNA ( Asp ) ( which has a dissimilar anticodon ) , by monitoring the formation of AcPhePhe , AcPheLeu or AcPheAsp , respectively . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The conformation change of Thermus thermophilus tRNA ( 1Ile ) upon complex formation with T . thermophilus elongation factor Tu ( EF Tu ) was studied by analysis of the circular dichroism ( CD ) bands at 315 nm ( due to the 2 thioribothymidine residue in the T loop ) and at 295 nm ( due to the core structure of tRNA ) . ^^^ Formation of the ternary complex of isoleucyl tRNA ( 1Ile ) and EF Tu . ^^^ These indicate the importance of the gamma phosphate group of GTP and the aminoacyl group in the formation of the active complex of aminoacyl tRNA and EF Tu . ^^^ Conformational changes of aminoacyl tRNA and uncharged tRNA upon complex formation with polypeptide chain elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Genes for the plastid elongation factor Tu and ribosomal protein S 7 and six tRNA genes on the 73 kb DNA from Astasia longa that resembles the chloroplast DNA of Euglena . ^^^ The genes for the plastid elongation factor Tu ( tufA ) and the ribosomal protein S 7 ( rps 7 ) , six tRNA genes ( trnQ , trnS , trnG , trnM , trnT , trnR ) , and three open reading frames were identified . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Yeast Met tRNA ( iMet ) lacking the modification of nucleoside 64 forms ternary complexes with GTP and elongation factor Tu from Escherichia coli . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Crosslinking of tRNA containing a long extra arm to elongation factor Tu by trans diamminedichloroplatinum ( 2 ) . ^^^ A tRNA containing a long extra arm , namely E . coli tRNA ( Leu 1 ) has been crosslinked to elongation factor Tu , with the crosslinking reagent trans diamminedichloroplatinum ( 2 ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Interaction of a selenocysteine incorporating tRNA with elongation factor Tu from E . coli . ^^^ The equilibrium dissociation constant for the interaction of Ser tRNA ( Sec ) ( UCA ) with elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| When the ribosome binds a deacylated tRNA at the E site ( in addition to a tRNA at the P site ) , the A site can not be occupied by AcPhe tRNA at 0 degree C and only poorly by the ternary complex elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Using the protection of EF Tu : GTP against spontaneous hydrolysis of the aminoacylester bond of Met tRNAfMet , we confirm these results , and show that the protection is specific for the non formylated form of the initiator tRNA . ^^^ The pattern of initiator tRNA protection by EF Tu against ribonuclease digestion is not significantly different from the one found previously for elongator tRNAs . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We have determined several kinetic parameters for the reaction of poly ( U ) programmed ribosomes with ternary complexes of elongation factor Tu , GTP , and yeast Phe tRNA analogs with different bases substituted for uridine in position 33 . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Upon monitoring the tRNA isoacceptor distribution by affinity chromatography on immobilized elongation factor Tu and subsequent two dimensional gel electrophoresis , a preferential synthesis of particular lysine and threonine accepting tRNAs was observed upon mitogenic stimulation . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The binding of Met tRNA ( fMet ) to ribosomes carrying fMet tRNA ( fMet ) in the P site is strongly stimulated by elongation factor EF Tu : GTP in the presence of ( AUG ) 3 . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Two genes , tufA and tufB , located at 73 and 88 minutes of the Escherichia coli linkage map , code for the polypeptide chain elongation factor EF Tu . tufB is transcribed with four upstream tRNA genes , thrU , tyrU , glyT and thrT , into a cotranscript of approximately 1800 nucleotides . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Control of the tRNA tufB operon in Escherichia coli . 1 . rRNA gene dosage effects and growth rate dependent regulation . ' Ribosome feedback ' effects on the expression of the genes specifying tRNA and EF Tu in E . coli have been studied at increased rrnB doses ( rRNA gene doses ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Raising the cellular EF Tu content , by introducing a multicopy plasmid encoding EF TuA into the cell , repressed the level of EF TuB but left the content of tRNA ( Thr ) 3 , encoded by the tRNA tufB operon , unaffected . ^^^ The molecular ratio of chromosome borne tufA and tufB transcripts also remained unaltered under conditions of excess EF Tu , though experiments with a tRNA tufB ' : lacZ operon fusion showed a decrease of tufB transcripts . ^^^ Surprisingly , addition of EF Tu to a coupled transcription / translation systems was found to block transcription initiation at the primary promoter of the tRNA tufB operon by over 90 % . ^^^ Although this in vitro effect of EF Tu could not be demonstrated in vivo , possibly because of a difference in higher order structure between plasmid borne and chromosome borne DNA , it indicates that under certain conditions EF Tu binds very specifically to the tRNA tufB operon promoter or its upstream region . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Crosslinking of elongation factor Tu to tRNA ( Phe ) by trans diamminedichloroplatinum ( 2 ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Modification of Bacillus subtilis elongation factor Tu by N tosyl L phenylalanyl chloromethane abolishes its ability to interact with the 3 ' terminal polynucleotide structure but not with the acyl bond in aminoacyl tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The main results are : ( 1 ) The cleavage rate of S 1 protein strongly depends on the cooperative effect of poly ( U ) and tRNA : ( 2 ) The conformation of L7 / L12 proteins is modulated by interaction of elongation factors with the ribosome and depends on hydrolysis of GTP ; ( 3 ) The sensitivity of some ribosomal proteins ( S 6 , S 7 , S 18 , S 19 , L 9 , L 16 , L 19 , and L 27 ) to proteases changes upon binding of EF Tu and depends on the ribosome functional state in accordance with GTP hydrolysis . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Different sites of the tRNA molecule influence the activity of the elongation factor Tu ( EF Tu ) center for GTP hydrolysis [ Parlato , G . , Pizzano , R . , Picone , D . , Guesnet , J . , Fasano , O . , & Parmeggiani , A . ( 1983 ) J . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Interaction of elongation factor Tu from Escherichia coli with aminoacyl tRNA carrying a fluorescent reporter group on the 3 ' terminus . ^^^ The product [ AEDANS s2C ] aminoacyl tRNA , forms a ternary complex with Escherichia coli elongation factor Tu and GTP , leading to up to 130 % fluorescence enhancement of the AEDANS chromophore . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The interactions of tRNA species with aminoacyl tRNA synthetases and polypeptide chain elongation factor Tu from Thermus thermophilus HB 8 were studied by the analyses mainly of the circular dichroism band of 2 thioribothymidine in position 54 of T . thermophilus tRNA species . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Interaction of the elongation factor EF Tu with the antibiotic kirromycin results in activation of the GTPase center of the factor and in induction of an additional tRNA binding site ( tRNA binding site 2 to distinguish it from the classical tRNA binding site 1 ) . ^^^ First , a strong correlation is observed between stimulation of the GTPase activity and enhancement of the reactivity of Cys 81 of EF Tu toward N ethylmaleimide at various concentrations of aminoacyl tRNA , deacylated tRNA , and N acetylaminoacyl tRNA . ^^^ EF Tu 10 GTP thus treated has lost its ability to protect the ester bond of aminoacyl tRNA . ^^^ GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Through this comparative structural analysis we have predicted the general location of functional domains in EF 1 alpha which interact with GTP and tRNA . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Methylation in vivo of elongation factor EF Tu at lysine 56 decreases the rate of tRNA dependent GTP hydrolysis . ^^^ Whereas tRNA binding at the classical binding site of EF Tu ( site 1 ) also appears not to be affected by the methylation of the protein , tRNA binding at site 2 is . ^^^ Although the apparent affinity of tRNA for site 2 remains unaltered upon methylation of EF Tu , the conformational effects of tRNA binding at this site become different . ^^^ Both the GTPase activity of the protein and the reactivity of Cys 81 are significantly less stimulated by the tRNA when EF Tu is methylated . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A fragment of the Pseudomonas aeruginosa genome contains five tRNA genes , four of which are linked to an EF Tu gene . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Affinity labeling at the A site of Escherichia coli ribosomes by a non hydrolyzable gamma amide analog of GTP . gamma Amides of GTP and affinity and photoaffinity derivatives of gamma amides of GTP : gamma anilide of GTP , gamma ( 4 azido ) anilide of GTP , gamma [ N ( 4 azidobenzyl ) N methyl ] amide of GTP , gamma [ 4 N ( 2 chloroethyl ) N methylaminobenzyl ] amide of GTP and gamma [ 4 N ( 2 oxoethyl ) N methylaminobenzyl ] amide of GTP substituted efficiently for GTP in the EF Tu dependent transfer of aminoacyl tRNA to the ribosome but , in contrast to GTP , they were not hydrolyzed in this process . ^^^ The radioactive analog of GTP : gamma [ 4 N ( 2 chloroethyl ) N methylamino [ 14C ] benzyl ] amide of GTP was used as an affinity labeling probe for the identification of components of the GTPase center formed in the EF Tu dependent transfer reaction of aminoacyl tRNA to the ribosomal A site . ^^^ Within a six component complex of poly ( U ) programmed E . coli ribosomes with elongation factor Tu , Phe tRNA ( Phe ) ( at the A site ) , tRNA ( Phe ) ( at the P site ) and the [ 14C ] GTP analog , mainly the ribosomal 23S RNA and to a lesser extent the ribosomal proteins L 17 , L 21 , S 16 , S 21 and the ribosomal 16S RNA were labeled by the reagent . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The complex formation between elongation factor Tu ( EF Tu ) , GTP , and valyl tRNAVal1A has been investigated in a hepes buffer of `` pH ' ' 7 . 4 and 0 . 2 M ionic strength using the small angle neutron scattering method at concentrations of D2O where EF Tu ( 42 % D2O ) and tRNA ( 71 % D2O ) are successively matched by the solvents . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The most extensive regions of SUF12 / EF 1 alpha homology are those regions that have been conserved in the EF 1 family , including domains involved in GTP and tRNA binding . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Trans diamminedichloroplatinum ( 2 ) was used to induce reversible crosslinks between EF Tu and Phe tRNA ( Phe ) within the ternary EF Tu / GTP / Phe tRNA ( Phe ) complex . ^^^ Crosslinking of elongation factor Tu to tRNA ( Phe ) by trans diamminedichloroplatinum ( 2 ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The fidelity of protein synthesis depends on the rate constants for the reaction of ribosomes with ternary complexes of elongation factor Tu ( EF Tu ) , GTP , and aminoacyl ( aa ) tRNA . ^^^ By measuring the rate constants for the reaction of poly ( U ) programmed ribosomes with a binary complex of elongation factor ( EF Tu ) and GTP we have shown that two of the key rate constants in the former reaction are determined exclusively by ribosome EF Tu interactions and are not affected by the aa tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor Tu within the ternary complex does not contribute to the binding of Phe tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We investigated the elongation factor Tu ( EF Tu ) dependent binding of Phe tRNA and Phe tRNAs with the nicks at positions 46 , 37 , and 17 to the Escherichia coli 70S ribosome poly ( U ) tRNAPhe complex . ^^^ A . 68 , 1796 ] , the EF Tu ribosome GTPase mediated by Phe tRNA is not inhibited by thiostrepton ; rather , the drug stimulates the endogenous GTPase of the EF Tu 10 70S ribosome . ^^^ Phe tRNA fragments 47 76 , 38 76 , and 17 76 all promote the EF Tu 10 GTPase reaction in the presence of 70S ribosome poly ( U ) tRNAPhe yeast . ^^^ Moreover , since the GTPase promoting activities of both the short and long fragments are similar , it appears that the most important aminoacyl transfer ribonucleic acid ( aa tRNA ) interaction with EF Tu occurs alongside its 3 ' quarter . ^^^ Aminoacyl tRNA elongation factor Tu ribosome interaction leading to hydrolysis of guanosine 5 ' triphosphate . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Our results suggest that the middle and C terminal domain play an essential role in regulating the activity of the N terminal domain of the intact molecule as well as in the interactions of EF Tu with aminoacylated tRNA , elongation factor Ts , and kirromycin . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| As expected from one of the functional roles of the 42 S particles ( tRNA binding , protection against deacylation and exchange with the ribosome ) , the amino acid sequence of thesaurin a was found to be closely related to that of the elongation factor EF 1 alpha . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A modified Met tRNAfMet which has a C 1 G72 base pair binds much more strongly to immobilized EF Tu 10 GTP than the native aminoacyl ( aa ) tRNA with non base paired C1A72 at this position , demonstrating that the base pair including the first nucleotide in the tRNA is one of the essential structural requirements for the aa tRNA 10 EF Tu 10 GTP ternary complex formation . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Binding of acetylvalyl tRNA to the P site was codon dependent and that of valyl tRNA to the A site was both codon and elongation factor Tu ( EFTu ) dependent . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Serine isoaccepting tRNAs were isolated from bulk tRNA of Escherichia coli by affinity chromatography on immobilized bacterial elongation factor Tu and their relative abundance was determined . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Determination of picomole quantities of eukaryotic amino acyl tRNA with bacterial elongation factor Tu : the extent of in vivo acylation of tRNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The GTPase activity of mutant EF Tu in the presence of aminoacyl tRNA and ribosome . mRNA is much higher than with wild type EF Tu and also much less dependent on the presence of mRNA . ^^^ In the preceding article a mutant elongation factor Tu ( EF TuD 2216 ) resistant to the action of kirromycin was found to display a spontaneous guanosine 5 ' triphosphatase ( GTPase ) activity , i . e . , in the absence of aminoacyl transfer ribonucleic acid ( tRNA ) and ribosome messenger RNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Discrimination between aminoacyl groups on su+ 7 tRNA by elongation factor Tu . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Modification characteristics of the tRNA in the free state , in the ternary complex with elongation factor EF Tu and GTP and in the ribosomal A and P sites were compared . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Escherichia coli Phe tRNA , modified with the photoaffinity reagent 6 ( 2 nitro 4 azidophenylamino ) caproate on the 3 ( 3 amino 3 carboxypropyl ) uridine residue , was crosslinked to E . coli EFTu Section upon irradiation at 0 degree C with visible light at wavelengths greater than 400 nm . ^^^ Binding of the tRNA to EFTu was a prerequisite for crosslinking , because neither EFTu . ^^^ GDP nor AcPhe tRNA could substitute ; EFTu . ^^^ Extensive peptide bond formation with AcPhe tRNA in the P site occurred despite the presence of the crosslinked EFTu . ^^^ We conclude that hydrolysis of GTP is sufficient to release the 3 ' end of the Phe tRNA from complexation with EFTu . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The deletion of the three tRNA genes does not significantly alter the in vivo expression of tufB as assessed by the kirromycin sensitive phenotype of the transformant cells and by the synthesis of EF Tu in mini cells . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Binding to the ribosomal A site was achieved enzymatically using the elongation factor Tu and GTP in the presence of deacylated tRNA which blocks the ribosomal P site . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The binding of the ternary complexes [ Phe tRNA 10 EF Tu 10 GTP ] and [ Pro tRNA 10 EF Tu 10 GTP ] to the programmed ribosomes was studied . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Irradiation ( 310 to 340 nm ) of probe modified Phe tRNA or Val tRNA placed in the ribosomal A site led to crosslinking that was totally dependent on irradiation , the presence of the azido group on the probe , mRNA , and elongation factor Tu ( EFTu ) . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In contrast , a ternary complex ( aminoacyl tRNA elongation factor Tu . ^^^ This suggests that release factor and elongation factor Tu have overlapping binding sites but the A site binding domains of the release factor and tRNA are exclusive . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| There is no fluorescence increase when the epsilon A labeled tRNAPhe is complexed with phenylalanyl tRNA synthetase , elongation factor Tu , or ribosomes . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Isolation of tRNA isoacceptors by affinity chromatography on immobilized bacterial elongation factor Tu . ^^^ Immobilized elongation factor Tu 10 GDP could be converted to Tu 10 GTP , which is able to bind aminoacyl tRNA . ^^^ When bulk tRNA from E . coli , baker ' s yeast , or bovine liver was aminoacylated by one amino acid only , the resulting aminoacyl tRNA could be separated in one step from the rest of the tRNA using an affinity column of immobilized elongation factor Tu 10 GTP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The deacylation of aa tRNA was accelerated by glycerol and sucrose even in the presence of EF Tu 10 GTP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Cross linking of tRNA at two different sites of the elongation factor Tu . ^^^ Recently , we reported on the induction by kirromycin of two tRNA binding sites on elongation factor Tu . ^^^ To obtain independent information on the existence of these two sites and to characterize them further , 3 ' oxidized tRNA was cross linked to elongation factor Tu by [ 3H ] borohydride reduction . ^^^ The tRNA cross linking sites are in agreement with the idea of two different binding sites of tRNA on elongation factor Tu . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The method utilizes the specific recognition of aminoacyl tRNA for E . coli protein synthesis elongation factor Tu which has been immobilized on an affinity matrix . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Finally , the influence of the elongation factor Tu from B . stearothermophilus on the tRNA structure is discussed . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| These results indicate that only the acceptor T psi C arm of aa tRNA interacts directly with EF Tu . ^^^ Our data also suggest that EF Tu facilitates protein biosynthesis by ensuring that every aa tRNA is in a particular ( possibly the same ) conformation prior to initiation of the recognition process at the ribosomal complex . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The interaction of the polypeptide chain elongation factor Tu ( EF Tu ) with the antibiotic kirromycin and tRNA has been studied by measuring the extent of protein modification with N tosyl L phenylalanine chloromethylketone ( TPCK ) and N ethylmaleimide ( NEM ) . ^^^ Binding of aminoacyl tRNA added at increasing concentrations to a solution of 40 microM EF Tu . ^^^ Moreover , NEM modification also indicates an additional tRNA binding site on EF Tu . ^^^ The elongation factor Tu . kirromycin complex has two binding sites for tRNA molecules . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In terms of the three dimensional structure of tRNA established for yeast tRNAPhe , EF Tu covers the aa end , aa stem , T stem , and extra loop on the side of the L shaped tRNA that exposes the extra loop . . ^^^ The site of interaction of aminoacyl tRNA with elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The complex formation between Escherichia coli aminoacyl tRNA , elongation factor Tu and GTP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The model proposed is consistent with the facts about interactions of the protein L7 / L12 with the elongation factors ( EF Tu and EF G ) involved in tRNA binding and translocation , as well as with the data available on the participation of proteins S 3 , S 5 , S 10 , S 14 and S 19 in the formation of tRNA sites . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The method exploits the radiochemical purity of the transcript and relies on the binding of aminoacyl tRNA but not of uncharged tRNA to purified elongation factor EF Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The data have been used for a schematic description of the structure of a part of the aminoacyl tRNA binding site of the bacterial elongation factor Tu . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| One of the four subunits of bacteriophage Q beta RNA replicase is elongation factor Tu ( EF Tu ) , the host aminoacyl tRNA ( AA tRNA ) binding protein . ^^^ To determine whether the RNA polymerase activity requires the tRNA binding site of EF Tu , we reconstituted replicase with EF Tu . ^^^ This cross linked ternary complex ( XLTC ) was formed by the reaction of N epsilon bromoacetyl Lys tRNA with EF Tu GTP . ^^^ Replicase reconstituted with XLTC was resolved from replicase containing EF Tu by chromatography on phosphocellulose , a result which confirmed that the tRNA moiety was incorporated into the enzyme . ^^^ From these results , it appears that the AA tRNA binding site on EF Tu is not required for the assembly or activity of Q beta RNA replicase . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| GTP valyl tRNA Val 1 complex is larger ( R = 3 . 6 nm ) than that of EF Tu . ^^^ From this model it is indicated that the acceptor stem of tRNA is attached to EF Tu and that the anticodon stem and loop protrude into the solution . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| This aminoacyl tRNA binds enzymatically ( in the presence of elongation factor Tu and GTP ) and nonenzymatically to the A site and is then transferred to the P site , if that site is free . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| These variations are likely to reduce the stability of the tRNA inside the cell or , among others , to interfere with the ability of the tRNA to functionally interact with elongation factor Tu and with the ribosome . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A nuclease protection assay was used to obtain equilibrium dissociation constants of Thermus thermophilus EF Tu with two well characterized internal deletions of Escherichia coli Ala tRNA ( Ala ) and yeast Phe tRNA ( Phe ) . ^^^ However , the Ala minihelix , where residue A 7 is joined directly to A 49 , binds to EF Tu less well than the full sized Ala tRNA ( Ala ) . ^^^ After six rounds of enrichment , two groups of RNA were obtained that bound T . thermophilus EF Tu as well as Ala tRNA ( Ala ) . ^^^ The selected RNAs bind EF Tu better than the minihelix either because they provide additional function groups for protein binding or because they have a structure more similar to the aminoacyl acceptor branch of tRNA . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Two elongation factors drive the ribosomal elongation cycle ; elongation factor 1 alpha ( EF 1 alpha ) mediates the binding of an aminoacyl tRNA to the ribosomal A site , whereas elongation factor 2 ( EF 2 ) catalyzes the translocation reaction . ^^^ EF 3 is essential for EF 1 alpha dependent A site binding of amino acyl tRNA only when the E site is occupied with a deacylated tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Although the 3 ' O anthraniloyl labeled tRNA does not seem to be functionally active , as far as the aminoacyl charging activity is concerned , surprisingly we found that it is able to form the ternary complex with elongation factor Tu ( EF Tu ) and GTP with an affinity consistently higher than uncharged tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| To estimate the affinity of tRNA toward EF Tu , Kd and K 1 were measured by the nuclease protection assay , and it was shown that the absence of modifications decreases ternary complex stability less than 2 fold . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The mechanisms by which elongation factor Tu ( EF Tu ) promotes the binding of aminoacyl tRNA to the A site of the ribosome and , in particular , how GTP hydrolysis by EF Tu is triggered on the ribosome , are not understood . ^^^ The steps following GTP hydrolysis the switch of EF Tu to the GDP bound conformation , the release of aminoacyl tRNA from EF Tu to the A site , and the dissociation of EF Tu GDP from the ribosome which are altogether suppressed by kirromycin , are not distinguished kinetically . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The distance between the corner of the L shaped transfer RNA and the GTP bound to elongation factor Tu ( EF Tu ) in the aminoacyl tRNA . ^^^ This large distance limits the possible arrangements of the EF Tu and the tRNA in the ternary complex . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^ Macromolecular arrangement in the aminoacyl tRNA . elongation factor Tu . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In its active GTP bound state EF Tu binds aminoacylated tRNA ( aa tRNA ) forming the ternary complex EF Tu : GTP : aa tRNA . ^^^ The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA , GTPase activity is induced and inactive EF Tu : GDP is released . ^^^ Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF Tu : GDPNP and yeast Phe tRNA ( Phe ) after its purification by HPLC . . ^^^ Purification and crystallization of the ternary complex of elongation factor Tu : GTP and Phe tRNA ( Phe ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Conformational transitions of Phe tRNA ( Phe ) that take place during elongation factor Tu ( EF Tu ) dependent binding to the A site of Escherichia coli ribosomes were followed by transient fluorescence measurements . ^^^ The latter conformational state is short lived , and the aminoacyl tRNA refolds during the following rearrangement that occurs after GTP hydrolysis and accompanies the release of the aminoacyl tRNA from EF Tu . ^^^ Transient conformational states of aminoacyl tRNA during ribosome binding catalyzed by elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Each is active as a complex with GTP . eEF 1 is a multimer and mediates the binding of the cognate aminoacyl tRNA to the ribosome , while eEF 2 , a monomer , catalyses the movement of the ribosome relative to the mRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor 1 ( EF 1 ) consists of four subunits : the alpha subunit catalyzes the GTP dependent binding of aminoacyl tRNA to ribosomes while the beta , gamma , and delta subunits catalyze GDP / GTP exchange on EF 1 alpha . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In the GTP form of the molecule , EF Tu binds tightly to aminoacyl tRNA , forming a ternary complex that interacts with the ribosomal acceptor site . ^^^ CONCLUSION : GTP binding by EF Tu leads to dramatic conformational changes which expose the tRNA binding site . ^^^ It appears that tRNA binding to EF Tu induces a further conformational change , which may affect the GTPase activity . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Escherichia coli elongation factor Tu mutants with decreased affinity for aminoacyl tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The affinity for aminoacyl ( aa ) tRNA and the intrinsic GTPase activity of the mutant EF Tu were decreased whereas the response of its GTPase center to aa tRNA was strongly increased . ^^^ These results suggest that the region around His 118 is involved in the binding of aa tRNA and in the transmission of a turn off signal generated by the interaction with aa tRNA and directed to the GTPase center of EF Tu . . ^^^ Histidine 118 of elongation factor Tu : its role in aminoacyl tRNA binding and regulation of the GTPase activity . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl tRNA in a ternary complex . tRNA ( Val ) from Escherichia coli was aminoacylated with [ 1 13C ] valine and its complex with Thermus thermophilus elongation factor EF Tu . ^^^ The results suggest that the aminoacyl residue of the valyl tRNA in ternary complex with bacterial EF Tu and GTP is not attached to tRNA by a regular ester bond to either a 2 ' or 3 ' hydroxyl group ; instead , an intermediate orthoester acid structure with covalent linkage to both vicinal hydroxyls of the terminal adenosine 76 is formed . ^^^ Mutation of arginine 59 located in the effector region of EF Tu , a conserved residue in protein elongation factors and the alpha subunits of heterotrimeric guanine nucleotide binding regulatory proteins ( G proteins ) , abolishes the stabilization of the orthoester acid structure of aminoacyl tRNA . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| An RNase protection assay was used to show that the dissociation rate constants and equilibrium constants of unmodified yeast and Escherichia coli phenylalanyl tRNA ( Phes ) to elongation factor Tu from E . coli were very similar to each other and to their fully modified counterparts . ^^^ The affinity of aminoacylated tRNA to elongation factor Tu was substantially lower when GTP analogues were used in place of GTP , emphasizing the importance of the beta gamma phosphate linkage in the function of G proteins . ^^^ Fourteen different mutations in conserved and semi conserved nucleotides of yeast phenylalanyl tRNA ( Phe ) were tested for binding to elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In the present paper we use Pb2+ ions as a functional probe to determine whether this part of tRNA is protected by the Escherichia coli elongation factor EF Tu in the ternary complex formed between Phe tRNAPhe and EF Tu . ^^^ Our results show that for tRNA in complex with EF Tu : GTP , the phosphodiester bond after D 17 is cleaved , yet the phosphodiester bonds after D 16 and G 15 are not . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Whereas the 5 ' phosphoribosyl residue prevents the binding of Met tRNA ( iMet ) to eEF 1 alpha , it does not influence the interaction with eIF 2 . ^^^ After removal of the ribosyl group , the demodified initiator tRNA showed binding to eEF 1 alpha , but no change was detected with respect to the interaction with the initiation factor eIF 2 . ^^^ This observation is interpreted to mean that a single modification of an eucaryotic initiator tRNA in yeast serves as a negative discriminant for eEF 1 alpha , thus preventing the initiator tRNA ( iMet ) from entering the elongation cycle of protein biosynthesis . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Discrimination against misacylated tRNA by chloroplast elongation factor Tu . ^^^ Whereas chloroplast Glu tRNA ( Glu ) is efficiently bound by this factor , the misacylated Glu tRNA ( Gln ) does not interact with chloroplast elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| There are genes for the 16S , 5S , and 23S rRNAs of the 70S chloroplast ribosomes , 27 different tRNA species , 21 ribosomal proteins plus the gene for elongation factor EF Tu , three RNA polymerase subunits , and 27 known photosynthesis related polypeptides . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We find that mutant ribosomes are impaired in EF Tu dependent binding of aminoacyl tRNA in vitro ; in contrast , nonenzymatic binding of tRNA to the A and P sites is unaffected , indicating that the defect involves an EF Tu related function rather than tRNA ribosome interactions per se . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The first step in the sequence of interactions between the ribosome and the complex of elongation factor Tu ( EF Tu ) , GTP , and aminoacyl tRNA , which eventually leads to A site bound aminoacyl tRNA , is the codon independent formation of an initial complex . ^^^ Hence , the ribosome induced GTP hydrolysis by EF Tu is strongly affected by the presence of the tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Purification of aminoacyl tRNA by affinity chromatography on immobilized Thermus thermophilus EF Tu . ^^^ Elongation factor Tu from Thermus thermophilus containing six histidine residues on its C terminus , EF Tu ( CHis 6 ) , was used for purification of aminoacyl tRNA isoacceptors , from aminoacylated bulk tRNA , by affinity chromatography . ^^^ Compared to alternative methods , the reported immobilization by C terminal histidine residues does not lead to loss of EF Tu ' s affinity for aminoacyl tRNA . ^^^ Elongation factor Tu from Thermus thermophilus containing six histidine residues on its C terminus , EF Tu ( CHis 6 ) , was used for purification of aminoacyl tRNA isoacceptors , from aminoacylated bulk tRNA , by affinity chromatography . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In this paper we have verified a possible interaction between rabbit aminoacyl tRNA synthetase and homologous translation elongation factor 1 alpha ( EF 1 alpha ) , the proteins which may play a role of sequential components involved in the transfer of the aminoacyl tRNA along the protein synthetic metabolic chain . ^^^ The stimulation of the phenylalanyl tRNA synthetase activity by EF 1 alpha is found . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In the A site , cleavages were found in the 2555 2573 region of 23S rRNA , around bases previously shown to be protected by A site tRNA , and in the alpha sarcin loop , the site of interaction of elongation factors EF Tu and EF G . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| EF Tu GTP can still form a stable complex with aminoacyl tRNA ( aa tRNA ) , but it no longer protects aa tRNA against spontaneous deacylation , showing that the EF Tu GTP orientation with respect to the 3 ' end of aa tRNA is modified . ^^^ However , the EF Tu dependent binding of aa tRNA to the ribosomal A site is impaired only slightly by the antibiotic and the activity of the peptidyl transferase center , as determined by puromycin reactivity , is not affected . ^^^ Thus , enacyloxin IIa can affect both EF Tu and the ribosomal A site directly , inducing an anomalous positioning of aa tRNA , that inhibits the incorporation of the amino acid into the polypeptide chain . ^^^ EF Tu GTP can still form a stable complex with aminoacyl tRNA ( aa tRNA ) , but it no longer protects aa tRNA against spontaneous deacylation , showing that the EF Tu GTP orientation with respect to the 3 ' end of aa tRNA is modified . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl tRNA . ^^^ Two residues of Escherichia coli elongation factor Tu involved in binding of aminoacyl tRNA were identified and subjected to mutational analysis . ^^^ The results verify our structural analysis of elongation factor Tu in complex with aminoacyl tRNA , which suggested an important role of Lys 89 and Asn 90 in tRNA binding . ^^^ Their functional roles are discussed in relation to the structure of elongation factor Tu in complex with aminoacyl tRNA . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| These observations strongly suggest that the electrophoretic retardation of the charged species reflects an aminoacylation induced conformational change of the 3 ' end of these mt tRNAs , with possible significant implications in connection with the known role of the acceptor end in tRNA interactions with the ribosomal peptidyl transferase center and the elongation factor Tu . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Functionally , EF 3 stimulates EF 1 alpha dependent binding of aminoacyl tRNA to the ribosomal A site when E site is occupied by deacylated tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Several mutant EF Tu species display altered behaviour towards aminoacyl tRNA with interesting effects on translational accuracy . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Steady state levels of mRNAs for EF 1 alpha F 1 and F 2 , of mRNAs for four ribosomal proteins , of total poly A+ RNA , rRNA , and tRNA were measured . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A moderate overexpression of EFTu is enough to lead to a misappropriation of initiator tRNA in the elongation process , whereas overproduced IF 2 allows the initiation of translation to occur with unformylated tRNA species . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| This change is presumably involved in triggering the release of tRNA , and EF Tu , from the ribosome . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Based on similarities between eukaryotic eIF 2gamma proteins and eubacterial EF Tu proteins , we previously proposed a major role for the gamma subunit in binding guanine nucleotide and tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In addition , the tRNA recognition properties of EF Tu and peptidyl tRNA hydrolase are considered . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor Tu ( EF Tu ) from Escherichia coli carrying the mutation G222D is unable to hydrolyze GTP on the ribosome and to sustain polypeptide synthesis at near physiological Mg2+ concentration , although the interactions with guanine nucleotides and aminoacyl tRNA are not changed significantly . ^^^ Here we report a pre steady state kinetic study of the binding of the ternary complexes of wild type and mutant EF Tu with Phe tRNA ( Phe ) and GTP to the A site of poly ( U ) programed ribosomes . ^^^ The main effect of the G222D mutation is the inhibition , at low Mg2+ concentration , of codon induced structural transitions of the tRNA and , in particular , their transmission to EF Tu that precedes GTP hydrolysis and the subsequent steps of A site binding . ^^^ The inhibition of the structural transitions is probably due to the interference of the negative charge introduced by the mutation with negative charges either of the 3 ' terminus of the tRNA , bound in the vicinity of the mutated amino acid in domain 2 of EF Tu , or of the ribosome . ^^^ Elongation factor Tu ( EF Tu ) from Escherichia coli carrying the mutation G222D is unable to hydrolyze GTP on the ribosome and to sustain polypeptide synthesis at near physiological Mg2+ concentration , although the interactions with guanine nucleotides and aminoacyl tRNA are not changed significantly . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The recent determination of the structure of the ternary complex of aminoacyl tRNA , EF Tu and a GTP analogue shows how the CCA end of all aminoacyl tRNA structures can be accommodated in a specific binding site on EF Tu GTP , and how part of the T helix can be recognized by EF Tu in a non sequence specific way . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The immobilized EF Tu maintained most of the guanosine nucleotide binding activity , but its ability to bind aminoacyl tRNA depended on the type of complex used in the coupling reaction . ^^^ GTP . aminoacyl tRNA . kirromycin complex yielded an immobilized factor that was much more active in binding aminoacyl tRNA than that obtained by coupling EF Tu . ^^^ GTP and the release of aminoacyl tRNA from the matrix bound EF Tu by GDP . ^^^ When total tRNA was aminoacylated by one amino acid only , a column of immobilized EF Tu GTP . kirromycin allowed the isolation of the aminoacylated tRNA from bulk tRNA . ^^^ Isolation of tRNA isoacceptors by affinity chromatography with immobilized elongation factor Tu from Escherichia coli . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Evidence for the formation of an unusual ternary complex of rabbit liver EF 1alpha with GDP and deacylated tRNA . ^^^ In this paper another ternary complex [ EF 1alpha * GDP * deacylated tRNA ] , never considered in widely accepted elongation schemes , is reported for the first time . ^^^ The formation of this unusual complex , postulated earlier ( FEBS Lett . ( 1996 ) 382 , 18 20 ) , has been detected by four independent methods . [ EF 1alpha * GDP ] interacting sites are located in the acceptor stem , TpsiC stem and TpsiC loop of tRNA ( Phe ) and tRNA ( Leu ) molecules . ^^^ Both tRNA and EF 1alpha are found to undergo certain conformational changes during their interaction . ^^^ The ability of EF 1alpha to form a complex with deacylated tRNA indicates that the factor may perform an important role in tRNA and aminoacyl tRNA channeling in higher eukaryotic cells . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The ternary complex of aminoacylated tRNA and EF Tu GTP . ^^^ The refined crystal structure of the ternary complex of yeast Phe tRNAPhe , Thermus aquaticus elongation factor EF Tu and the non hydrolyzable GTP analog , GDPNP , reveals many details of the EF Tu recognition of aminoacylated tRNA ( aa tRNA ) . ^^^ EF Tu GTP recognizes the aminoacyl bond and one side of the backbone fold of the acceptor helix and has a high affinity for all ordinary elongator aa tRNAs by binding to this aa tRNA motif . ^^^ Subtle rearrangements of the binding pocket may occur to optimize the fit to any side chain of the aminoacyl group and interactions with EF Tu stabilize the 3 ' aminoacyl isomer of aa tRNA . ^^^ A general complementarity is observed in the location of the binding sites in tRNA for synthetases and for EF Tu . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The effect on readthrough by changing these 1 and 2 codons is different on the two forms of tRNA ( Trp ) and is also dependent on the structure of EF Tu . ^^^ Together with mutant EF Tu , both forms of tRNA ( Trp ) are sensitive . ^^^ This interaction is changed by mutation in tRNA ( Trp ) at position 24 or in EF Tu at position 375 . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The recently solved structure of the ternary complex formed between GTP bound elongation factor Tu and aminoacylated tRNA reveals that the elements of aminoacyl tRNA that interact with elongation factor Tu can be divided into three groups : the T stem ; the 3 ' end CCA Phe ; and the 5 ' end . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The defective phenotype resulting from the ts22b16 mutation can be corrected by over expressing either the mitochondrial elongation factor EF Tu or the mutated form of the tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The structure indicates that the conserved glutamic acid at position 271 in Thermus aquaticus EF Tu could be involved in the binding of the 3 ' CCA Phe end of the aminoacylated tRNA . ^^^ Determination of the crystal structure of the ternary complex formed between elongation factor Tu : GTP and aminoacylated tRNA revealed three regions of interaction between elongation factor Tu and tRNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Recognition of the universally conserved 3 ' CCA end of tRNA by elongation factor EF Tu . ^^^ To better understand the function of the 3 ' CCA sequence of tRNA in protein synthesis , the effects of systematically varying all three bases on formation of the Val tRNA ( Val ) : EF Tu : GTP ternary complex were investigated . ^^^ Substitutions at C 74 and C 75 have no significant effect , but replacing A 76 with pyrimidines decreases the affinity of valyl tRNA ( Val ) for EF Tu : GTP , thus explaining the inability of these tRNA ( Val ) variants to function in polypeptide synthesis . ^^^ Valyl tRNA ( Val ) terminating in 3 ' guanine is readily recognized by EF TU : GTP . ^^^ Dissociation constants of the EF Tu : GTP ternary complexes with valine tRNAs having nucleotide substitutions at the 3 ' end increase in the order adenine < guanine < uracil ; EF Tu has very little affinity for tRNA terminating in 3 ' cytosine . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Fitting the crystal structure of EF G GDP into the cryo density map reveals a large conformational change mainly associated with domain 4 , the domain that mimics the shape of the anticodon arm of the tRNA in the structurally homologous ternary complex of Phe tRNAPhe , EF Tu , and a GTP analog . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In Escherichia coli , selenocysteine biosynthesis and incorporation into selenoproteins requires the action of four gene products , including the specialized selenocysteine tRNA ( Sec ) and elongation factor SELB , different from the universal EF Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Since it mimics the structure of the ternary complex of EF Tu : GTP with aminoacyl tRNA , which subsequently binds to the ribosome , EF G : GDP leaves an imprint on the ribosome for the ternary complex . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The model of `` molecular mimicry between release factors and tRNA ' ' predicts that eRF 1 mimics tRNA to read the stop codon and that eRF 3 mimics elongation factor EF Tu to bring eRF 1 to the A site of the ribosome for termination of protein synthesis . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The pattern of tRNA interaction observed for EF 1alpha ( eEF1A ) therefore closely resembles that of bacterial EF Tu ( EF1A ) . . ^^^ GTP binding to aminoacyl tRNAs , aminoacyl viral RNA , and tRNA shows close correspondence to the RNA binding properties of EF Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Functional interaction of mammalian valyl tRNA synthetase with elongation factor EF 1alpha in the complex with EF 1H . ^^^ In this study , we have examined the possibility that the functioning of the companion enzyme EF 1alpha could regulate valyl tRNA synthetase activity . ^^^ We show here that the addition of EF 1alpha and GTP in excess in the aminoacylation mixture is accompanied by a 2 fold stimulation of valyl tRNAVal synthesis catalyzed by the valyl tRNA synthetase component of the ValRS . ^^^ Since valyl tRNA synthetase and elongation factor EF 1alpha catalyze two consecutive steps of the in vivo tRNA cycle , aminoacylation and formation of the ternary complex EF 1alpha . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| By comparing the obtained 3D model to that of EF Tu : Phe tRNAPhe crystalline complex in which the 5 ' phosphate of the ligand also lies between a K and an R side chain , we propose that , in both systems , the capacity of the 5 ' phosphate of a tRNA to reach or not a receptor site is the main identity element governing generic selection of elongator tRNAs . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Since then , high resolution structures have been reported for RNA complexes with five other tRNA synthetases , the elongation factor Tu , the bacteriophage MS 2 coat protein , the human spliceosomal U1A and U2B ' ' U1A ' proteins , and the HIV 1 nucleocapsid protein . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| MA was found to interact with elongation factor 1 alpha ( EF1alpha ) , an essential component of the translation machinery that delivers aminoacyl tRNA to ribosomes . ^^^ The Gag EF1alpha interaction appears to be mediated by RNA , in that basic residues in MA and NC are required for binding to EF1alpha , RNase disrupts the interaction , and a Gag mutant with undetectable EF1alpha binding activity is impaired in its ability to associate with tRNA in cells . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| EF 1alpha , which transports the aminoacyl tRNA to the ribosome , is a member of the G protein superfamily . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The discovery that three domains of elongation factor G are structurally mimicking the amino acylated tRNA in the ternary complex of elongation factor Tu has been the basis of much discussion of the functional similarities and functional differences of elongation factor Tu and elongation factor G in their interactions with the ribosome . ^^^ Elongation factor G : GDP is now thought to leave the ribosome in a state ready for checking the codon anticodon interaction of the aminoacyl tRNA contained in the ternary complex of elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We examined the level of aminoacylation of amber suppressor tRNAAlawith respect to the method of isolating aminoacyl tRNA , the rate of cell growth , the cellular levels of alanine synthetase and elongation factor TU ( EF Tu ) , the amount of tRNA and the characteristics of EF Tu binding . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor Tu ( EF Tu ) provides the binding of aminoacylated tRNA to the ribosome and protects the aminoester bond against hydrolysis until a correct match between the codon on mRNA and the anticodon on tRNA can be achieved . ^^^ The structural results provide a rather complete picture of the major structural forms of EF Tu , including the so called ternary complex of aa tRNA : EF Tu : GTP . ^^^ Elongation factor Tu ( EF Tu ) provides the binding of aminoacylated tRNA to the ribosome and protects the aminoester bond against hydrolysis until a correct match between the codon on mRNA and the anticodon on tRNA can be achieved . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In EF Tu GTP , Thr 382 in domain 3 has a strategic position in the interface with domain 1 ; it is hydrogen bonded to Glu 117 that takes part in the switch 2 mechanism , and is close to the T stem binding site of the tRNA , in a region known for many kirromycin resistance mutations . ^^^ In reverse , phosphorylated EF Tu has an increased affinity for EF Ts , does not bind kirromycin and can no longer bind aminoacyi tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Using three dimensional cryoelectron microscopy , the binding positions of tRNA and elongation factors EF G and EF Tu ( the latter complexed with aminoacyl tRNA and GTP ) on the ribosome were determined in previous studies . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Together with prior biochemical studies , the structural findings confirm that GE2270A inhibits protein synthesis by blocking the GDP to GTP conformational change and by directly competing with aminoacyl tRNA for the same binding site on EF Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The effect of mutations in EF Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability . ^^^ One method is based on EF Tu protection of the tRNA 3 ' acceptor end against RNase A cleavage and yields the Kd value together with the corresponding dissociation and association rate constants from one single set of experiments . ^^^ It is based on competition between EF Tu species with and without a ( His ) 6 extension for the same aminoacyl tRNA and yields a relative Kd value . ^^^ Raising the assay temperature from 4 to 37 degrees C causes a 30 fold increase of Kd for EF Tu 10 GTP 10 Phe tRNA complexes . ^^^ Elongation factor Tu is essential for binding and a correct delivery of aminoacyl tRNA during protein biosynthesis . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| This core has several layers of unusual base pairs , which are revealed by the recent crystal structure of the tRNA complexed with the elongation factor EF Tu and an analog of GTP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We have used two RNA fragments , one which contains the anticodon and D hairpin domains ( ACD oligomer ) derived from tRNA ( Phe ) and the second which comprises the acceptor stem and T hairpin domains derived from tRNA ( Ala ) ( AST oligomer ) that aminoacylates with alanine and forms a ternary complex with EF Tu . ^^^ These results suggest that codon recognition as such is not sufficient for GTPase activation and that an intact tRNA molecule is required for transmitting the signal created by codon recognition to EF Tu . . ^^^ Intact aminoacyl tRNA is required to trigger GTP hydrolysis by elongation factor Tu on the ribosome . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Kinetic parameters for tmRNA binding to alanyl tRNA synthetase and elongation factor Tu from Escherichia coli . ^^^ The association rate constant of Ala tmRNA for elongation factor Tu in complex with GTP is about 150 fold lower than that of Ala tRNA ( Ala ) , whereas its dissocation rate constant is about 5 fold lower . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The properties and role in peptide elongation of ATPase intrinsic to rat liver ribosomes were investigated . ( 1 ) Rat liver 80S ribosomes showed high ATPase and GTPase activities , whereas the GTPase activity of EF 1alpha and EF 2 was very low . mRNA , aminoacyl tRNA , and elongation factors alone enhanced ribosomal ATPase activity and in combination stimulated it additively or synergistically . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| To further understand the EF Tu ( mt ) subcycle , the dissociation constants for the release of aa tRNA from the ternary complex ( K ( tRNA ) ) and for the dissociation of the EF Tu . ^^^ Interaction of mitochondrial elongation factor Tu with aminoacyl tRNA and elongation factor Ts . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The G 15 G48 conformations differ significantly compared to that observed in the native tRNA ( Cys ) structure bound to EF Tu , further implicating an important role for surrounding nucleotides in maintaining the integrity of the tertiary core and its consequent ability to present crucial recognition determinants to aminoacyl tRNA synthetases . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The purpose of our study was to examine the expression of a cluster of genes that are required for translation in C . trachomatis serovar F : infA ( encoding Initiation Factor 1 ) , tRNA ( Thr ) , tuf ( encoding Elongation Factor Tu ) , and tRNA ( Trp ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The EF Tu complexed with GTP and aminoacyl tRNA delivers tRNA to the ribosome , whereas EF G stimulates translocation , a process in which tRNA and mRNA movements occur in the ribosome . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| These and previous results have led to a model in which the binding of eEF1A to the 3 ' end to antagonize minus strand initiation is a major role of the tRNA like structure . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| High level expression of non functional model proteins , derived from elongation factor EF Tu by the deletion of an essential domain , greatly inhibits the growth of Escherichia coli partly deficient in peptidyl tRNA hydrolase . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A : eEF1Balpha . ^^^ The second end of eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA aminoacyl end of the tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Identified genes encode components of the plastid transcriptional and translational machinery : genes for three subunits of a chloroplast RNA polymerase , 20 chloroplast ribosomal protein genes , a gene for a plastid elongation factor Tu , 27 plastidic tRNA genes and three tandemly arranged repeats of 16S , 23S and 5S rDNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The concept of the shuttle role of elongation factor eEF1A is grounded ; the factor , being in a GTP bound form , delivers aminoacyl tRNA to the ribosome and then , in the GDP form after hydrolysis of GTP on the ribosome , forms a complex with the deacylated tRNA and delivers it to the aminoacyl tRNA synthetase . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor SELB , whose amino terminal part shows homology to EF Tu , was found to be the key component mediating delivery of selenocysteyl tRNA ( Sec ) to the ribosomal A site . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Here , we show that EF Tu binds misacylated tRNAs over a much wider range of affinities than it binds the corresponding correctly acylated tRNAs , suggesting that the protein exhibits considerable specificity for both the amino acid side chain and the tRNA body . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| GDP have been identified that are located outside the tRNA part of tmRNA , indicating an unusual interaction of tmRNA with EF Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| GTP , it has been established that the valylated aminoacyl RNA domain , which in TYMV RNA is formed by the 3 ' half of the tRNA like region , is sufficient for complex formation with EF 1alpha . ^^^ It is also shown that the TYMV RNA replicase ( RNA dependent RNA polymerase ) isolated from TYMV infected Chinese cabbage leaves does not contain tRNA nucleotidyltransferase , valyl tRNA synthetase or EF 1alpha . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The native form of MetRS , containing the C terminal RNA binding domain , behaves as a processive enzyme ; release of the reaction product is not spontaneous , but may be synchronized with the subsequent step of the tRNA cycle through EF 1alpha assisted dissociation of Met tRNA ( Met ) . ^^^ It may ensure an efficient capture of tRNA ( Met ) under conditions of suboptimal deacylated tRNA concentration prevailing in vivo , and may instigate direct transfer of aminoacylated tRNA from the synthetase to elongation factor EF 1alpha . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| For Escherichia coli , previous studies on initial steps of this `` trans translation ' ' mechanism revealed that tmRNA alanylation by Ala tRNA synthetase and binding of Ala tmRNA by EF Tu GTP for subsequent delivery to stalled ribosomes are inefficient when compared to analogous reactions with canonical tRNA ( Ala ) . ^^^ Interaction with SmpB and EF Tu was also observed at the acceptor arm of Ala tRNA ( Ala ) , but there the alanylation efficiency was inhibited rather than stimulated by SmpB . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| EF 1alpha 10 GTP catalyzes the binding of aminoacyl tRNA to the A site of the ribosome . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The tRNA specificity of Thermus thermophilus EF Tu . ^^^ The E . coli elongator tRNAs exhibit a wide range of binding affinities that varied from 11 . 7 kcal / mol for Val tRNA ( Glu ) to 8 . 1 kcal / mol for Val tRNA ( Tyr ) , clearly establishing EF Tu * GTP as a sequence specific RNA binding protein . ^^^ Because EF Tu is known to contact only the phosphodiester backbone of tRNA , the observed specificity must be a consequence of an indirect readout mechanism . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| This rotation , driven by a conformational change in elongation factor Tu involving GTP hydrolysis , transorients the incoming tRNA into the A site from the D site of initial binding and decoding , where it can be proofread and accommodated . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In eukaryotes , the eukaryotic translation elongation factor eEF1A responsible for transporting amino acylated tRNA to the ribosome forms a higher order complex , eEF1H , with its guanine nucleotide exchange factor eEF1B . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| During the elongation cycle of protein biosynthesis , the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl tRNA , elongation factor Tu and GTP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| In bacteria , the C terminal part of SelB recognizes this hairpin , while the N terminal part binds GTP and tRNA in analogy with elongation factor Tu ( EF Tu ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The translation elongation factor Tu ( EF Tu ) delivers aminoacyl tRNAs to ribosomes by recognizing the tRNA acceptor and T stems . ^^^ EF Tu 2 seems unique in its amino acid specificity because it recognizes the aminoacyl moiety of seryl tRNAs and the tRNA structure itself . ^^^ Such EF Tu evolution might explain tRNA structural divergence in animal mitochondria . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Multimolecular complexes involving the eukaryotic elongation factor 1A ( eEF1A ) have been suggested to play an important role in the channeling ( vectorial transfer ) of tRNA during protein synthesis [ Negrutskii , B . ^^^ Recently we have demonstrated that besides performing its canonical function of forming a ternary complex with GTP and aminoacyl tRNA , the mammalian eEF1A can produce a noncanonical ternary complex with GDP and uncharged tRNA [ Petrushenko , Z . ^^^ GDP . tRNA ] and [ eEF1A . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The structures of eubacterial release factors are not yet known , and the first example of tRNA mimicry was discovered when elongation factor G ( EF G ) was found to have a closely similar shape to a complex of elongation factor Tu ( EF Tu ) with aminoacyl tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The mRNA codon in the ribosomal A site is recognized by aminoacyl tRNA ( aa tRNA ) in a ternary complex with elongation factor Tu ( EF Tu ) and GTP . ^^^ The aa tRNA interacts with 16S rRNA , helix 69 of 23S rRNA and proteins S 12 and L 11 , while the sarcin ricin loop of 23S rRNA contacts domain 1 of EF Tu near the nucleotide binding pocket . ^^^ Ribosome interactions of aminoacyl tRNA and elongation factor Tu in the codon recognition complex . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Exp 5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| According to the neutron scattering data , eEF1A becomes much more compact in the complex with uncharged tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Models predict eEF 3 affects the delivery of cognate aminoacyl tRNA , a function performed by eEF1A , by removing deacylated tRNA from the ribosomal Exit site . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Thus , we were able to show a direct link between the vital tRNA binding property of EF Tu and polymerase activity . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| On the basis of the E . coli trpA 34 missense mutant transformed with heterologous ND aspS genes , we developed a system with which to measure the in vivo formation of Asp tRNA ( Asn ) and its acceptance by elongation factor EF Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Human aspartyl tRNA synthetase ( hDRS ) contains an extension at the N terminus , which is involved in the transfer of Asp tRNA to elongation factor alpha 1 ( EF1alpha ) . ^^^ Following Asp tRNA transfer to EF1alpha , the peptide assumes the folded conformation . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Requirement of modified residue m1A9 for EF Tu binding to nematode mitochondrial tRNA lacking the T arm . ^^^ Although the unmodified A . suum mt Met tRNA ( Met ) did not bind to nematode mt EF Tu , the m1A9 containing tRNA bound to the EF Tu , suggesting that m1A at position 9 is necessary for binding of nematode mt tRNAs lacking the T arm to the EF Tu , probably because of maintenance of the L shape like structure or interaction with the C terminal amino acid residues of the EF Tu . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Atypical archaeal tRNA pyrrolysine transcript behaves towards EF Tu as a typical elongator tRNA . ^^^ This indicates that no antideterminant sequence is present in the body of the tRNA ( Pyl ) transcript to prevent it from interacting with EF Tu , in contrast with the otherwise functionally similar tRNA ( Sec ) that mediates selenocysteine incorporation . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The pathogenic A4269G mutation in human mitochondrial tRNA ( Ile ) alters the T stem structure and decreases the binding affinity for elongation factor Tu . ^^^ In addition , measurements of the binding affinity of the aminoacylated mutant tRNA ( Ile ) for mt elongation factor Tu ( EF Tu ) showed that the mutant tRNA ( Ile ) binds mt EF Tu less efficiently than the wild type does . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The fate of the glutamylated tRNA ( Asp ) is not known , but its incapacity to bind elongation factor Tu suggests that it is not involved in ribosomal protein synthesis . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The affinity of elongation factor Tu for an aminoacyl tRNA is modulated by the esterified amino acid . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We suggest that the p methoxyphenyl ring of these cyclic depsipeptides is inserted into the same pocket in eEF1A that normally lodges either the 3 ' terminal adenine of aminoacylated tRNA , as inferred from two prokaryotic EF Tu . ^^^ GTP . tRNA complexes , or the aromatic side chain of Phe / Tyr 163 from the nucleotide exchange factor eEF1Balpha , as observed in several 10 ray crystal structures of a yeast eEF1A : eEF1Balpha complex . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| An in vitro analysis of the effects of the argU 10 ( Ts ) mutation on tRNA functions revealed that the affinity with elongation factor Tu GTP of the argU 10 ( Ts ) mutant tRNA is impaired at 30 and 43 degrees C , and this defect is more serious at the higher temperature . ^^^ We concluded that the phenotypic properties of the argU 10 ( Ts ) mutant result from these reduced intracellular levels of the tRNA , which are probably caused by the defective interactions with elongation factor Tu and arginyl tRNA synthetase . . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Fluorescence resonance energy transfer was used to observe aminoacyl tRNA ( aa tRNA ) stably accommodating into the aminoacyl site ( A site ) of the ribosome via a multistep , elongation factor Tu dependent process . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Aminoacyl tRNA ( aa tRNA ) is delivered to the ribosome in a ternary complex with elongation factor Tu ( EF Tu ) and GTP . ^^^ The stepwise movement of aa tRNA from EF Tu into the ribosomal A site entails a number of intermediates . ^^^ The ribosome recognizes aa tRNA through shape discrimination of the codon anticodon duplex and regulates the rates of GTP hydrolysis by EF Tu and aa tRNA accommodation in the A site by an induced fit mechanism . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We sequenced varying length regions of the following genes : ( 1 ) elongation factor 1alpha ( Ef1alpha ; 1028 bp ) ; ( 2 ) tektin ( tektin ; 715 bp ) ; ( 3 ) wingless ( wg ; 405 bp ) ; ( 4 ) ribosomal protein L 5 ( RpL 5 ; 722 bp , exons 1 , 2 , 3 , and introns 1 and 2 ) ; and ( 5 ) mitochondrial cytochrome oxidase 1 , 2 ( Co 1 and Co 2 and intervening leucine tRNA ; 1599 bp ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Like the translational elongation factor EF Tu , RNase P interacts with a large number of substrates where RNase P with its RNA subunit generates tRNAs with matured 5 ' termini by cleaving tRNA precursors immediately 5 ' of the residue at +1 , i . e . at the position that corresponds to the first residue in tRNA . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The adaptor molecule of translation is tRNA , but the delivery of aminoacyl tRNAs the primary substrate of the ribosome relies on the formation of a ternary complex with elongation factor Tu ( EF Tu ) and GTP . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| It resembles elongation factor EF 1 A and ensures interaction with Met tRNA ( 1 ) ( Met ) . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Recent biochemical and structural data make it possible to understand at least in outline the structural basis for tRNA selection , in which codon recognition by cognate tRNA results in the hydrolysis of GTP by EF Tu over 75 A away . ^^^ Part of the additional binding energy of cognate tRNA is used to induce conformational changes in the ribosome that stabilize a transition state for GTP hydrolysis by EF Tu and subsequently result in accelerated accommodation of tRNA into the peptidyl transferase center . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| We show that , in Bacillus cereus , the two LysRSs together aminoacylate a small RNA of unknown function named tRNA ( Other ) , and that the aminoacylated product stably binds translation elongation factor Tu . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Moreover , YbaK can not compete for aminoacyl tRNAs in the presence of elongation factor Tu , suggesting that YbaK acts before release of the aminoacyl tRNA from the synthetase . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The two data sets can also be used to calculate the free energy of binding of EF Tu to any misacylated E . coli tRNA , and the values agree well with previously published experimental values . ^^^ |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| A unique tRNA recognition mechanism of Caenorhabditis elegans mitochondrial EF Tu 2 . ^^^ EF Tu 2 specifically recognizes Ser tRNA ( Ser ) that lacks a D arm but has a short T arm . ^^^ Our previous study led us to speculate the lack of the D arm may be essential for the tRNA recognition of EF Tu 2 . ^^^ The hydrolysis protection assay using several EF Tu 2 mutants then strongly suggests that seven C terminal amino acid residues of EF Tu 2 are essential for its aminoacyl tRNA binding activity . ^^^ Our results indicate that the formation of the nematode mitochondrial ( mt ) EF Tu2 / GTP / aminoacyl tRNA ternary complex is probably supported by a unique interaction between the C terminal extension of EF Tu 2 and the tRNA . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor Tu ( EF Tu ) binds GTP and aminoacyl tRNA ( aa tRNA ) forming a ternary complex which is delivered to the A site of the ribosome . ^^^ Elongation factor Tu ( EF Tu ) binds GTP and aminoacyl tRNA ( aa tRNA ) forming a ternary complex which is delivered to the A site of the ribosome . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF Tu . ^^^ We further demonstrate that deacylated tRNA is released from the E site by binding a ternary complex aminoacyl tRNA * EF Tu * GDPNP to the A site . ^^^ This observation indicates that the E tRNA is released after the decoding step but before both GTP hydrolysis by EF Tu and accommodation of the A tRNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor Tu ( EF Tu ) is responsible for the aminoacyl tRNA binding to the ribosomal A site , while elongation factor G ( EF G ) catalyses translocation of mRNA in the ribosome by one codon , accompanied by tRNA movement between the binding sites . ^^^ Elongation factor Tu ( EF Tu ) is responsible for the aminoacyl tRNA binding to the ribosomal A site , while elongation factor G ( EF G ) catalyses translocation of mRNA in the ribosome by one codon , accompanied by tRNA movement between the binding sites . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Recent structural and biochemical experiments indicate that bacterial elongation factor Tu and the ribosomal A site show specificity for both the amino acid and the tRNA portions of their aminoacyl tRNA ( aa tRNA ) substrates . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Glu tRNA is either bound to elongation factor Tu to enter protein synthesis or is reduced by glutamyl tRNA reductase ( GluTR ) in the first step of tetrapyrrole biosynthesis in most bacteria , archaea and in chloroplasts . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A : GTP : Phe tRNA ( Phe ) complex . ^^^ Comparison with the EF1A structure suggests that only the gamma subunit of the aIF2alphagamma heterodimer contacts tRNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The tRNAs were either free or bound to the proteins involved in translation : aminoacyl tRNA and elongation factor EF Tu . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The polyalanine synthesis system attained by using a tmRNA variant consisting of only the tRNA like domain revealed that it was completely dependent on the presence of SmpB and greatly enhanced by EF Tu and EF G . ^^^ Based on these results , we suggest that SmpB structurally mimics the anticodon arm of tRNA and elicits GTP hydrolysis of EF Tu upon tmRNA accommodation in the A site of the ribosome . . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Pulvomycin inhibits protein synthesis by preventing the formation of the ternary complex between elongation factor Tu ( EF Tu ) 10 GTP and aa tRNA . ^^^ The structure of the T . thermophilus EF Tu 10 GDPNP 10 GE 2270 A complex at 1 . 6 A resolution shows that GE 2270 A interferes with the binding of the 3 ' aminoacyl group and part of the acceptor stem of aa tRNA but not with the 5 ' end . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Among these , we have identified the gene for the mitochondrial protein synthesis elongation factor EF Tu and the specific mt aminoacyl tRNA synthetases . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| The tight aminoacyl tRNA product binding by class 1 enzymes correlates with the ability of EF Tu to form a ternary complex with class 1 but not class 2 synthetases , and the further capacity of this protein to enhance the rate of aminoacylation by class 1 synthetases . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Elongation factor eEF 3 is an ATPase that , in addition to the two canonical factors eEF1A and eEF 2 , serves an essential function in the translation cycle of fungi . eEF 3 is required for the binding of the aminoacyl tRNA eEF1A GTP ternary complex to the ribosomal A site and has been suggested to facilitate the clearance of deacyl tRNA from the E site . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| However , in Caenorhabditis elegans mitochondria , two distinct EF Tu species , EF Tu 1 and EF Tu 2 , recognize 20 species of T armless tRNA and two species of D armless tRNA ( Ser ) , respectively . ^^^ We previously reported that C . elegans mitochondrial EF Tu 2 specifically recognizes the serine moiety of serylated tRNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| Our previous study showed that nematode Caenorhabditis elegans EF Tu 1 binds specifically to T armless tRNA . ^^^ In this study , the recognition mechanism of T armless tRNA by EF Tu 1 was investigated . ^^^ Both modification interference assays and primer extension analysis of cross linked ternary complexes revealed that EF Tu 1 interacts not only with the tRNA acceptor stem but also with the D arm . ^^^ This is the first example of an EF Tu recognizing the D arm of a tRNA . ^^^ The binding activity of EF Tu 1 was impaired by deletion of only 14 residues from the C terminus , indicating that the C terminus of EF Tu 1 is required for its binding to T armless tRNA . ^^^ |
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| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O14717 and P68104 |
Pubmed |
SVM Score :0.0 |
| NA |
|