Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.95985755 |
Further characterization of eIF 5 demonstrates that eIF 5 specifically associates with eIF 2 , forming an eIF 2 . eIF 5 complex . 0.95985755^^^ Purification and characterization of bacterially expressed mammalian translation initiation factor 5 ( eIF 5 ) : demonstration that eIF 5 forms a specific complex with eIF 2 . 0.55492902^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.82513289 |
Further characterization of mutant eIF 5 showed that the mutant protein , expressed in Escherichia coli , is defective both in its interaction with eIF 2 as well as in mediating the hydrolysis of GTP bound to the 40S initiation complex and consequently in the formation of the 80S initiation complex . 0.82513289^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
In contrast , when 60 S ribosomal subunits were also present in an eIF 5 catalyzed reaction , the eIF 2 . ^^^ In contrast , when 60 S ribosomal subunits were preincubated with either free eIF 2 or with eIF 2 . eIF 2B complex and then added to a reaction containing both the 40 S initiation complex and eIF 5 , the eIF 2 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Because of the highly catalytic activity of eIF 5 in initiation reactions , the presence of even low levels of eIF 5 in eIF 2 preparations causes hydrolysis of GTP bound to the 40 S initiation complex . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Incubation of a 40 S initiation complex with eIF 5 , in the presence or absence of 60 S ribosomal subunits at 25 degrees C , causes rapid and quantitative hydrolysis of ribosome bound GTP to form an eIF 2 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
The following activities have been detected : eIF 2 , eIF3 / 4F , eIF4A , eIF4B , eIF4C , eIF4D , and eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Evidence is presented that eIF 5 mediated hydrolysis releases the GTP bound to the 40 S initiation complex as an intact eIF 2 10 GDP complex rather than as free GDP and eIF 2 which subsequently recombine to form the binary complex . ^^^ Furthermore , formation and release of eIF 2 10 GDP from the ribosomal complex do not require concomitant formation of an 80 S initiation complex since both reactions occur efficiently when the 40 S initiation complex reacts with eIF 5 in the absence of 60 S ribosomal subunits . ^^^ These results , along with the observation that the 40 S initiation complex formed with the nonhydrolyzable analogue of GTP , 5 ' guanylylmethylene diphosphonate , can neither join a 60 S ribosomal subunit nor releases ribosome bound eIF 2 , suggest that following eIF 5 mediated hydrolysis of GTP bound to the 40 S initiation complex , both Pi and eIF 2 10 GDP complex are released from ribosomes prior to the joining of 60 S ribosomal subunits to the 40 S initiation complex . . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Histones ( H 1 , H2A B , H 3 , and H 4 ) and protein synthesis initiation factors other than eIF 2 ( eIF 3 , eIF 4A , eIF 4B , and eIF 5 ) were not substrates or were very poor substrates for the purified dsRNA dependent protein kinase . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Five initiation factors , eIF 2 , eIF 3 , eIF 4A , eIF 4B , and eIF 5 , were purified from human HeLa cells . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Several initiation factors ( eIF 2 , eIF 3 , eIF 4A , eIF 4B , eIF 4C , eIF 4E and eIF 5 ) and elongation factor 1 were found to have no such discriminatory effect . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Met tRNAi . 40S [ the complex between the 40S ribosomal subunit and the ternary complex containing equimolar amounts of eukaryotic initiation factor 2 ( eIF 2 ) , GTP , and eukaryotic initiator methionyl tRNA ( Met tRNAi ) ] with a 60S ribosomal subunit in the presence of mRNA , cap binding protein ( with `` capped ' ' messengers ) , ATP , and the initiation factors eIF 3 , eIF 4a , 4b , 4c , and eIF 5 , results in the formation of an 80S initiation complex ( Met tRNAi . 80S . mRNA ) with concomitant hydrolysis of GTP and liberation of eIF 2 for recycling in subsequent initiation events . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Using an assay system which requires all the initiation factors for optimal activity it was possible to show that the 0 40 % ammonium sulfate cut of initiation factors ( containing eIF 3 and eIF 4B ) was sensitive to helenalin , while the 40 50 % ammonium sulfate cut ( containing eIF 2 and eIF 5 ) was not . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
The effect of added deacylase on the labeling of 48 S complexes with [ 35S ] Met tRNAf can be overcome by adding eIF 5 or a soluble reticulocyte protein that has been termed the reversing factor , but not by the addition of eIF 2 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
It is hypothesized that the nucleotidyltransferase related domain is directly involved in the GDP / GTP exchange , whereas the C terminal conserved domain may be involved in the interaction of eIF 2B , eIF 4 gamma , and eIF 5 with eIF 2 . . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
The SUI 5 suppressor gene is identical to the TIF 5 gene that encodes eIF 5 , a translation initiation factor known to stimulate the hydrolysis of GTP bound to eIF 2 as part of the 43S preinitiation complex . ^^^ Biochemical characterization of SUI 3 suppressor alleles that encode mutant forms of the beta subunit of eIF 2 revealed that these mutant eIF 2 complexes have a higher intrinsic rate of GTP hydrolysis , which is eIF 5 independent . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Specific interaction of eukaryotic translation initiation factor 5 ( eIF 5 ) with the beta subunit of eIF 2 . ^^^ We observed that eIF 5 specifically interacted with the beta subunit of initiation factor eIF 2 . ^^^ Furthermore , both yeast and mammalian eIF 5 bind to the beta subunit of either mammalian or yeast eIF 2 . ^^^ GTP ternary complex , and ( b ) eIF 5 forms a specific complex with eIF 2 suggests that the specific interaction between eIF 5 and the beta subunit of eIF 2 may be critical for the hydrolysis of GTP during translation initiation . . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Conserved bipartite motifs in yeast eIF 5 and eIF2Bepsilon , GTPase activating and GDP GTP exchange factors in translation initiation , mediate binding to their common substrate eIF 2 . ^^^ In the initiation phase of eukaryotic translation , eIF 5 stimulates the hydrolysis of GTP bound to eIF 2 in the 40S ribosomal pre initiation complex , and the resultant GDP on eIF 2 is replaced with GTP by the complex nucleotide exchange factor , eIF2B . ^^^ We also find that three lysine rich boxes in the N terminal segment of eIF2beta mediate the binding of eIF 2 to both eIF 5 and eIF2B . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
The resulting complex requires eIF 1 , eIF1A , eIF4A , eIF4B and eIF4F to bind to a messenger RNA and to scan to the initiation codon . eIF 5 stimulates hydrolysis of eIF 2 bound GTP and eIF 2 is released from the 48S complex formed at the initiation codon before it is joined by a 60S subunit to form an active 80S ribosome . ^^^ Here we show that hydrolysis of eIF 2 bound GTP induced by eIF 5 in 48S complexes is necessary but not sufficient for the subunits to join . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Eukaryotic translation initiation factor 5 ( eIF 5 ) forms a complex with eIF 2 by interacting with the beta subunit of eIF 2 . ^^^ In this work , we show that , in addition to the eIF 2 beta binding region at the C terminus of eIF 5 , the N terminal region of eIF 5 is also required for eIF 5 dependent GTP hydrolysis . ^^^ Mutation of this arginine residue to alanine or even to conservative lysine caused a severe defect in the ability of eIF 5 to promote GTP hydrolysis from the 40 S initiation complex , although the ability of these mutant proteins to bind to eIF 2 beta remained unchanged . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
During translation initiation in eukaryotes , initiation factor eIF 5 is required for hydrolysis of GTP bound to eIF 2 ( the protein which brings the initiator Met tRNA ( 1 ) to the 40S subunit ) . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Conserved sequences in the beta subunit of archaeal and eukaryal translation initiation factor 2 ( eIF 2 ) , absent from eIF 5 , mediate interaction with eIF2gamma . ^^^ Here we provide a comparative sequence analysis of the beta subunit of eIF 2 and its archaeal counterpart ( aIF2beta ) . aIF2beta differs from eIF2beta in not possessing an N terminal extension implicated in binding RNA , eIF 5 and eIF2B . ^^^ Previously isolated mutations in the yeast eIF2beta , which allow initiation of translation at UUG codons due to the uncovering of an intrinsic GTPase activity in eIF 2 , involve residues that are conserved in aIF2beta , but not in eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Mutational analysis of mammalian translation initiation factor 5 ( eIF 5 ) : role of interaction between the beta subunit of eIF 2 and eIF 5 in eIF 5 function in vitro and in vivo . ^^^ Eukaryotic translation initiation factor 5 ( eIF 5 ) interacts with the 40S initiation complex ( 40S eIF 3 AUG Met tRNA ( f ) eIF 2 GTP ) to promote the hydrolysis of ribosome bound GTP . eIF 5 also forms a complex with eIF 2 by interacting with the beta subunit of eIF 2 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
A multifactor complex of eukaryotic initiation factors , eIF 1 , eIF 2 , eIF 3 , eIF 5 , and initiator tRNA ( Met ) is an important translation initiation intermediate in vivo . ^^^ The eIF 2 , eIF 5 , and eIF 1 all have been implicated in stringent selection of AUG as the start codon . ^^^ We show that yeast eIF 5 can bridge interaction in vitro between eIF 3 and eIF 2 by binding simultaneously to the amino terminus of eIF 3 subunit NIP 1 and the amino terminal half of eIF2beta , dependent on a conserved bipartite motif in the carboxyl terminus of eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
A multifactor complex of eIF 1 , eIF 2 , eIF 3 , eIF 5 , and tRNA ( 1 ) Met promotes initiation complex assembly and couples GTP hydrolysis to AUG recognition . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
We show that affinity tagged RLI 1 co purifies with eukaryotic translation initiation factor 3 ( eIF 3 ) , eIF 5 , and eIF 2 , but not with other translation initiation factors or with translation elongation or termination factors . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Multiple roles for the C terminal domain of eIF 5 in translation initiation complex assembly and GTPase activation . eIF 5 stimulates the GTPase activity of eIF 2 bound to Met tRNA ( 1 ) ( Met ) , and its C terminal domain ( eIF 5 CTD ) bridges interaction between eIF 2 and eIF3 / eIF1 in a multifactor complex containing Met tRNA ( 1 ) ( Met ) . ^^^ In vivo , tif 5 7A eliminated eIF 5 as a stable component of the pre initiation complex and led to accumulation of 48S complexes containing eIF 2 ; thus , conversion of 48S to 80S complexes is the rate limiting defect in this mutant . ^^^ We propose that eIF 5 CTD stimulates binding of Met tRNA ( 1 ) ( Met ) and mRNA to 40S subunits through interactions with eIF 2 , eIF 3 and eIF4G ; however , its most important function is to anchor eIF 5 to other components of the 48S complex in a manner required to couple GTP hydrolysis to AUG recognition during the scanning phase of initiation . . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Joining of 48S complexes to 60S subunits to form 80S ribosomes requires eIF5B , which has an essential ribosome dependent GTPase activity and hydrolysis of eIF 2 bound GTP induced by eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
First , eIF 5 promotes hydrolysis of GTP only when the nucleotide is bound to eIF 2 in the 40S initiation complex . eIF 5 , by itself , does not hydrolyze either free GTP or GTP bound to the Met tRNAf . eIF 2 . ^^^ Second , as with typical GAPs , eIF 5 forms a complex with eIF 2 , the GTP binding protein . ^^^ This interaction , which occurs between the lysine rich N terminal region of the beta subunit of eIF 2 and the glutamic acid rich C terminal region of eIF 5 , is essential for eIF 5 function both in vitro and in vivo in yeast cells . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
In addition to the contact between eIF 2 and the N terminal domain ( NTD ) of NIP 1 bridged by eIF 5 , the C terminal domain ( CTD ) of TIF 32 binds eIF 2 directly and is required for eIF 2 eIF3 association in vivo . ^^^ Overexpressing a CTD less form of TIF 32 exacerbated the initiation defect of an eIF 5 mutation that weakens the NIP 1 eIF5 eIF 2 connection . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
We found that the vast majority of translation initiation factors ( eIF 2 , eIF2B , eIF 3 , eIF4A1 , eIF 5 and eIF5B ) , all three elongation factors ( eEF1A , eEF1B and eEF 2 ) and the termination factor eRF 1 are strictly excluded from nuclei . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Initiation factor 3 ( eIF 3 ) forms a multifactor complex ( MFC ) with eIF 1 , eIF 2 , and eIF 5 that stimulates Met tRNA ( 1 ) ( Met ) binding to 40S ribosomes and promotes scanning or AUG recognition . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
In vivo , overexpression of eIF 2 and tRNA ( Met ) ( 1 ) suppresses the temperature sensitive phenotype of tif 5 7A altering eIF 5 CTD by increasing interaction of the mutant eIF 5 with eIF 2 by mass action and restoring its defective interaction with eIF 3 . ^^^ We propose that the primary function of eIF 5 CTD is to serve as an assembly guide by rapidly promoting stoichiometric MFC assembly with the aid of eIF 2 while excluding formation of nonfunctional complexes . . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Interestingly , we found that TC resides in a multifactor complex ( MFC ) with eIF 3 , eIF 1 , and the GTPase activating protein for eIF 2 , known as eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Six of the point mutations derepressed GCN 4 translation independent of eIF 2 phosphorylation ( Gcd phenotype ) at a permissive temperature , directly implicating eIF 5 CTD in the eIF2 / GTP / Met tRNA ( 1 ) Met ternary complex binding process required for GCN 4 translational control . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Mutation at Ser 2 and Ser 67 did not affect eIF2beta integrating into the eIF 2 trimer or being able to complex with eIF 5 and CK2alpha . ^^^ The eIF2beta CT form was also incorporated into the eIF 2 trimer but did not bind to eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
We show here that the human ABCE 1 protein is essential for in vitro and in vivo translation of mRNA and that it binds to eIF2alpha and eIF 5 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Recruitment of the eukaryotic translation initiation factor 2 ( eIF 2 ) GTP Met tRNAiMet ternary complex to the 40S ribosome is stimulated by multiple initiation factors in vitro , including eIF 3 , eIF 1 , eIF 5 , and eIF1A . ^^^ To define the factor requirements for these reactions in vivo , we examined the effects of depleting eIF 2 , eIF 3 , eIF 5 , or eIF4G in Saccharomyces cerevisiae cells on binding of the ternary complex , other initiation factors , and RPL41A mRNA to native 43S and 48S preinitiation complexes . ^^^ Depleting eIF 2 , eIF 3 , or eIF 5 reduced 40S binding of all constituents of the multifactor complex ( MFC ) , comprised of these three factors and eIF 1 , supporting a mechanism of coupled 40S binding by MFC components . 40S bound mRNA strongly accumulated in eIF 5 depleted cells , even though MFC binding to 40S subunits was reduced by eIF 5 depletion . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
GDP binds the pentameric factor eIF2B for guanine nucleotide exchange . eIF 5 and the eIF2Bvarepsilon catalytic subunit possess a conserved eIF 2 binding site . ^^^ Nearly half of cellular eIF 2 forms a complex with eIF 5 lacking Met tRNA ( 1 ) ( Met ) , and here we investigate its physiological significance . eIF 5 overexpression increases the abundance of both eIF2 / eIF5 and TC / eIF5 complexes , thereby impeding eIF2B reaction and MFC formation , respectively . eIF2Bvarepsilon mutations , but not other eIF2B mutations , enhance the ability of overexpressed eIF 5 to compete for eIF 2 , indicating that interaction of eIF2Bvarepsilon with eIF 2 normally disrupts eIF2 / eIF5 interaction . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
The factor eIF 5 stimulates hydrolysis of GTP by eIF 2 upon AUG codon recognition , whereas the factor eIF2B promotes guanine nucleotide exchange on eIF 2 to recycle the factor for additional rounds of translation initiation . ^^^ The GTP binding ( G ) domain resides in the gamma subunit of the heterotrimeric eIF 2 ; however , only eIF2beta , and not eIF2gamma , has been reported to directly bind to eIF 5 or eIF2B . ^^^ Consistently , an internal deletion of residues 50 100 of yeast eIF 5 impairs the interaction with recombinant eIF2gamma G domain and abolishes the ability of eIF 5 to stimulate eIF 2 GTPase activity in translation initiation complexes in vitro . ^^^ Thus , rather than allosterically regulating eIF2gamma G domain function via eIF2beta , our data support a model in which the GTPase activating factor eIF 5 and the guanine nucleotide exchange factor eIF2B modulate eIF 2 function through direct interactions with the eIF2gamma G domain . . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Interestingly , the N terminal subdomain of eIF 5 reveals an alpha / beta fold structurally similar to both the archaeal orthologue of the beta subunit of eIF 2 and , unexpectedly , to eIF 1 . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
Crystal structure of the C terminal domain of S . cerevisiae eIF 5 . eIF 5 , a GTPase activating protein ( GAP ) specific for eIF 2 , plays a critical role in pre initiation complex assembly and correct AUG selection during eukaryotic translation initiation . eIF 5 is involved in the formation of the multifactor complex ( MFC ) , an important intermediate of the 43S pre initiation complex . ^^^ |
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Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P55010 and P05198 |
Pubmed |
SVM Score :0.0 |
NA |
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