| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.72303337 |
| The schistosome HMG 2 like protein was found to bind preferentially to single stranded DNA . 0.72303337^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.54701894 |
| Thus , our results indicate that HMG 2 binds with high affinity to DNA modified with therapeutically active platinum compounds . 0.54701894^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :1.1430704 |
| Nonhistone protein HMG 2 , like HMG 1 , binds with B DNA in a sequence nonspecific manner and causes structural alterations in DNA such as bending , kinking and unwinding . 1.1430704^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.99324452 |
| HMGB 2 binds with linker DNA and / or the entry and exit of nucleosomes fixed at both ends likewise mini circles similar to alpha DNA and beta DNA . 0.99324452^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Localization of the binding region of high mobility group protein 2 to cisplatin damaged DNA . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Supercoil dependent recognition of specific DNA sites by chromosomal protein HMG 2 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| High mobility group proteins HMG 1 and HMG 2 do not decrease the melting temperature of DNA . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Isolated HMG 1 and HMG 2 fractions showed DNA unwinding activity of similar extents . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| DNA sequence and structure of a trout HMG 2 gene . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| We show that the DNA bending proteins HMG 1 and HMG 2 stimulate cleavage and RAG protein binding at the 23 bp spacer signal . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Deletion of the HP 1 or HMG 2 binding domain had no effect on DNA binding . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Interaction of a non histone chromatin protein ( high mobility group protein 2 ) with DNA . 1 . ^^^ The interaction with DNA of the calf thymus chromatin non histone protein termed the high mobility group protein 2 has been studied by sedimentation analysis in the ultracentrifuge and by measuring the binding of the 125I labelled protein to DNA . ^^^ Although the binding parameters are similar for these two proteins , high mobility group protein 2 differs from high mobility group protein 1 in that the former appears to change the shape of the DNA to a more compact form . 2 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Nonhistone proteins HMG 1 and HMG 2 unwind DNA double helix . ^^^ In a previous communication we have shown that both HMG 1 and HMG 2 nonhistone proteins change the DNA helical structure and the binding of HMG 1 and HMG 2 to DNA induces a net unwinding equivalent of DNA double helix ( Javaherian , K . , Liu , L . ^^^ Employing melting absorption technique , we now show that in the presence of salt HMG 1 and HMG 2 destabilize DNA whereas in the absence of salt , they both stabilize DNA molecules . ^^^ These results together suggest that HMG 1 and HMG 2 unwind DNA double helix by local denaturation of the DNA base pairs . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| This soluble ( S ) fraction was relatively depleted in H 1 histones and methylated DNA ( 5 methylcytosine ) but highly enriched in RNA , single stranded DNA , and nonhistone chromosomal proteins , particularly two species of the high mobility group identified as HMG 1 and HMG 2 . ^^^ The mononucleosomes appeared normal in terms of sedimentation behavior , DNA length , and content of histones H2A , H2B , H 3 , and H 4 , but lacked H 1 , and instead were associated with approximately stoichiometric amounts of HMG 1 and HMG 2 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Nonhistone proteins HMG 1 and HMG 2 change the DNA helical structure . ^^^ Two chromatin nonhistone proteins ( from calf thymus ) of the high mobility group , HMG 1 and HMG 2 , reduce the linking number ( topological winding number ) of a circular DNA if the covalent closure of the DNA is carried out in their presence . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Interaction of non histone chromosomal proteins HMG 1 and HMG 2 with DNA . ^^^ Interaction between non histone protein HMG 1 or HMG 2 and DNA has been studied by using thermal denaturation and circular dichroism ( CD ) spectroscopy . ^^^ There are 6 . 0 amino acids / nucleotide in HMG 1 bound DNA and 5 . 0 in HMGI bound DNA which suggests that each HMB 1 moleculae would cover about 20 base pairs of DNA and each HMG 2 molecule would cover about 25 base pairs . 3 . ^^^ DNA conformation is distorted only slightly by the binding of protein HMG 1 or HMG 2 . 5 . ^^^ Neither the melting nor the CD properties of HMG 1 DNA or HMG 2 DNA complexes differ substantially whether they are prepared by NaCl gradient dialysis in urea or by direct mixing of protein and DNA at 0 . 15 M NaCl , followed by dialysis against the same buffer i . e . 0 . 25 mM EDTA ( pH 8 . 0 ) . . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The amino acid sequences of two DNA binding domains , `` HMG box , ' ' also recently found in several transcription factors , are completely homologous in human and pig HMG 2 . ^^^ The present study , which is the first one on the isolation and characterization of complete gene coding for HMG 2 protein , may be useful for evolutional and genomic analysis of the proteins containing the HMG box sequences for DNA binding . . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The predicted amino acid sequence of ABF 2 is closely related to the high mobility group proteins HMG 1 and HMG 2 from vertebrate cell nuclei and to several other DNA binding proteins . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The effect of nonhistone protein HMG 1 and HMG 2 from pig thymus on the in vitro nucleosome assembly has been examined with plasmid pSV 2 gpt DNA and pig thymus core histones in the presence of DNA topoisomerase 1 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| HMG 1 and HMG 2 were exclusively dissociated from chromatin with 1 mM bleomycin under the solvent condition where the DNA strand breaking activity of the drug is repressed . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| DNA sequencing and Northern ( RNA ) blot analysis revealed that one gene , called ACP 2 ( acidic protein 2 ) , synthesizes a poly ( A ) + RNA in S . cerevisiae which encodes a 27 , 000 molecular weight protein whose amino acid sequence is homologous to those of calf HMG 1 and HMG 2 and trout HMGT proteins . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The amino acid sequence of the two yeast HMG CoA reductase isozymes was deduced from DNA sequence analysis of the HMG 1 and HMG 2 genes . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| A high mobility group ( HMG ) nonhistone protein fraction HMG ( 1+2 ) from pig thymus , composed of HMG 1 and HMG 2 , has an activity to unwind the double helical structure of DNA ( Yoshida , M . and Shimura , K . ( 1984 ) J . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Under low ionic conditions ( 2 mM Tris buffer plus EDTA ) addition of 1 2 molecules of HMG 2 per nucleosome markedly stabilized the segment of the linker DNA against thermal denaturation . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| These results indicated that the presence of the 40 50 base pairs long segment of the ' linker ' DNA in nucleosomes was not necessary for the establishment of mutual contacts of HMG 1 and HMG 2 proteins with core histones . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Differential binding of chromosomal proteins HMG 1 and HMG 2 to superhelical DNA . ^^^ The binding of chromosomal proteins HMG 1 and HMG 2 to various DNA structures was examined by a nitrocellulose filter binding assay using a 32P labelled supercoiled plasmid . ^^^ Binding assays and competition experiments indicated that HMG 2 has a higher affinity than HMG 1 for supercoiled DNA . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Unwinding of DNA by nonhistone protein HMG 1 and HMG 2 . ^^^ The enzyme kinetic studies with endonucleases specific for single stranded DNA and the thermal denaturation analyses of DNA showed that a high mobility group ( HMG ) nonhistone protein fraction HMG ( 1 + 2 ) , composed of HMG 1 and HMG 2 , has an activity to unwind DNA partially at low protein to DNA weight ratio . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The testis was distinguished in that it contained a substantially higher level of HMG 2 than any other rat tissue ( 32 micrograms / mg of DNA ) . ^^^ High levels of HMG 2 in the testis were due to pachytene spermatocytes and early spermatids ( 56 + / 4 and 47 + / 6 micrograms / mg of DNA , respectively ) . ^^^ Mixtures of spermatogonia and early primary spermatocytes showed lower levels of HMG 2 ( 12 + / 3 micrograms / mg of DNA ) similar to proliferating somatic tissues , whereas late spermatids had no detectable HMG proteins . ^^^ The somatic cells of the testis , including isolated populations of Sertoli and Leydig cells , showed very low levels of HMG 2 ( 2 micrograms / mg of DNA ) , similar to those in nonproliferating somatic tissues . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| It is concluded that HMG T lacks the highly acidic domain found in HMG 1 ( and HMG 2 ) that remains free from DNA under these conditions . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The rat liver single stranded DNA binding protein , S 25 and HD 25 , isolated by differential DNA cellulose affinity chromatography was compared to the high mobility group proteins , HMG 1 and HMG 2 , isolated from rat liver chromatin by the technique of Goodwin et al . ( Goodwin , G . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Following the second large acidic domain is another basic domain of 87 amino acids with significant sequence and structural homology to HMG 1 and HMG 2 DNA binding proteins . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Recently , DNA ring closure assays showed that high mobility group protein HMG 1 and its close homolog HMG 2 mediate sequence independent DNA flexion . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The interaction with HMG 2 results in a marked increase in the sequence specific DNA binding activity of the Oct proteins . ^^^ Interestingly , the HMG 2 protein is not present in the protein DNA complex detected by an electrophoretic mobility shift assay . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Northern analysis demonstrated that the level of HMG 2 mRNA was markedly enhanced in the post S phase and reached a maximum at G 2 phase , suggesting that expression of the HMG 2 gene is not coupled with DNA synthesis . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| HMG 2 expression is restricted to meristematic ( root tip and shoot apex ) and floral ( secretory zone of the stigma , mature pollen grains , gynoecium vascular tissue , and fertilized ovules ) tissues . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| A functional gene encoding high mobility group 2 ( HMG 2 ) protein , which is an abundant eukaryotic DNA binding protein , has been isolated . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The eukaryotic HMG 1 and HMG 2 proteins differ entirely in structure from HU but they also bind DNA non specifically and induce or stabilize deformed DNA . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| DNA PK activity determined with a synthetic peptide and alpha casein as substrates was stimulated several fold by HMG 1 , HMG 2 , and the DNA binding domains . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The nonspecific DNA binding and bending proteins HMG 1 and HMG 2 promote the assembly of complex nucleoprotein structures . ^^^ By use of ligase mediated circularization assays , we demonstrate that HMG 1 and HMG 2 can bend DNA extremely efficiently , forming circles as small as 66 bp , and even 59 bp circles at high HMG protein concentrations . ^^^ We suggest that an important biological function of HMG 1 and HMG 2 is to facilitate cooperative interactions between cis acting proteins by promoting DNA flexibility . ^^^ A general role for HMG 1 and HMG 2 in chromatin structure is also suggested by their ability to wrap DNA duplexes into highly compact forms . . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| In the presence of anti HMG 2 antibodies the DNA synthetic activity of oligodendrocyte nuclei in vitro was significantly decreased . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The open reading frame of this gene contains an 80 amino acid motif , the SRY box , which shares a high degree of homology with a DNA binding domain found in the high mobility group ( HMG ) proteins HMG 1 and HMG 2 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Replacement of Cys 45 or Cys 106 with a Ser residue reduced HMG 2 protein binding to CDDP DNA . ^^^ From these findings , we speculate that the intracellular oxidative environment could affect the redox state of protein thiols in HMG 1 and HMG 2 and in addition , regulate the ability of these proteins to recognize cis Pt DNA adduct formation in tumor cells . . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The 3 ' untranslated region of the HMG 2 axolotl cDNA is also similar to the avian and mammalian HMG 2 3 ' UT sequences , suggesting that some selective events have acted at the DNA level to conserve this region , which could be important in the differential expression of the HMG 1 and HMG 2 genes . ^^^ The axolotl HMG 2 protein contains the two well conserved HMG boxes which are thought to be the DNA binding domains of the molecule . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| We show here that GST fusion proteins of HMG domains from HMG 1 and HMG 2 promote a triple stranded complex formation between DNA containing the ( GGA / TCC ) 11 repeat and oligonucleotides of d ( GGA ) 11 probably due to G : G base pairing . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Differential binding of HMG 1 , HMG 2 , and a single HMG box to cisplatin damaged DNA . ^^^ The HMG box domain is a DNA binding domain present in the nonhistone chromosomal proteins HMG 1 and HMG 2 and in other proteins involved in the regulation of gene expression . ^^^ Previous studies have demonstrated that HMG 1 and HMG 2 bind with high affinity to DNA modified with the cancer chemotherapeutic drug cisplatin ( CDDP ) . ^^^ In this report , we compare the binding of full length HMG 1 and HMG 2 and the HMG boxes present in these proteins to that of CDDP DNA . ^^^ Complexes between HMG 1 , HMG 2 , or HMG Box A + B and CDDP DNA were stable at > or = 500 mM salt , while complexes between a single HMG box and CDDP DNA exhibited decreased stability . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| HMG 2 binds to Cr DNA with a calculated Kd of approximately 10 ( 9 ) M . ^^^ These results suggest that the covalent attachment of Cr to DNA induces alterations in DNA structure which are recognized by HMG 1 and HMG 2 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| This complex includes the proteins RAG 1 , RAG 2 , HMG 1 or the closely related HMG 2 protein , and the components of the DNA dependent protein kinase . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| HMG 2 is a DNA bending protein that is predominantly found in the nucleus in proliferating cells and in the cytoplasm of terminally differentiated cells . ^^^ We believe that the presence of HMG 2 in the enhancer promoter binding protein complex of cTnC augments DNA bending and facilitates the DNA binding and interaction of other tissue specific factors ( e . g . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The primary studies by gel retardation assay showed that HMG 2 has higher affinity than HMG 1 for supercoiled and linear DNA . ^^^ The DNA binding of HMG 2 appeared strong enough to allow exchange with HMG 1 molecule already bound to DNA , while the DNA binding region of HMG 1 showed higher affinity than that of HMG 2 . ^^^ The kinetic data indicated that the Kd for the complex of HMG 2 with DNA is smaller than that of HMG 1 , in contrast to the situation for the DNA binding region of these proteins . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Hence , it became obvious that the initial steps of the reaction are carried out by the lymphocyte specific proteins RAG 1 and RAG 2 ( recombination activating genes ) , with the help of members of the high mobility group protein family of DNA binding proteins , HMG 1 or HMG 2 . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The members of one such family , HMG 1 and HMG 2 , are ubiquitously expressed and facilitate the formation of nucleoprotein complexes where the DNA is sharply bent . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Here we show that HMG 1 and the highly related HMG 2 stimulate DNA binding by other steroid receptors , including estrogen , androgen , and glucocorticoid receptors , but have no effect on DNA binding by several nonsteroid nuclear receptors , including retinoid acid receptor ( RAR ) , retinoic 10 receptor ( RXR ) , and vitamin D receptor ( VDR ) . ^^^ Instead , the addition of purified RXR enhanced RAR and VDR DNA binding through a heterodimerization mechanism and HMG 1 or HMG 2 had no further effect on DNA binding by RXR RAR or RXR VDR heterodimers . ^^^ HMG 1 and HMG 2 ( HMG 1 / 2 ) themselves do not bind to progesterone response elements , but in the presence of PR they were detected as part of an HMG PR DNA ternary complex . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The HMG 2 domains ( A+B ) polypeptide devoid of the C terminal acidic region was more effective for DNA PKcs stimulation than the full length HMG 2 , and HMG 2 domain A and domain B polypeptides . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| As HMG 2 has DNA bending activity ( 6 ) , our data suggest that HMG proteins may augment DNA fragmentation during apoptosis through changes in chromosome structure . . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Differences in DNA recognition and conformational change activity between boxes A and B in HMG 2 protein . ^^^ To understand the mode of HMG 2 interaction with DNA , we expressed various HMG 2 peptides containing HMG1 / 2 box ( es ) in Escherichia coli cells and purified them . ^^^ Gel retardation and DNA supercoiling assay indicated that the region essential for the preferential binding of HMG 2 with negatively supercoiled DNA and DNA unwinding activity is located in box B , but not sufficient alone . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| By contrast , transcriptional activation by VP 16 was highest in the presence of HMG 2 as well as PC 4 and when DNA templates had linear topology . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Screening of cDNA libraries for the homologous vertebrate proteins high mobility group ( HMG ) 1 and 2 using DNA probes based on the coding sequences is likely to result in isolation of both HMG 1 and HMG 2 clones , as well as pseudogenes , which may be transcribed at low levels . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| This complex formation was subject to competition by CDDP treated non specific salmon sperm DNA , indicating that ectopic HMG 2 recognizes CDDP damaged DNA . ^^^ These results suggest that HMG 2 may enhance the CDDP sensitivity of cells by inhibiting repair of the DNA lesion induced by CDDP . . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The high mobility group ( HMG ) domain is a DNA binding motif found in the non histone chromosomal proteins , HMG 1 and HMG 2 , and some transcription factors . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The RAG 1 homeodomain recruits HMG 1 and HMG 2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA bending activity of RAG 1 RAG2 . 5 ( D ) J recombination is initiated by the specific binding of the RAG 1 RAG2 ( RAG1 / 2 ) complex to the heptamer nonamer recombination signal sequences ( RSS ) . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| DNA blot analysis revealed that hmg 1 and hmg 2 belong to small subfamilies that probably include homeologous loci in allotetraploid cotton ( Gossypium hirsutum L . ) . ^^^ |
|
| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The HMG domains of the chromosomal high mobility group proteins homologous to the vertebrate HMG 1 and HMG 2 proteins preferentially recognize distorted DNA structures . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| We have previously observed that double stranded DNA fragments containing a tract of the tandemly repeated sequence poly ( CA ) . poly ( TG ) can associate in vitro to form stable complexes of low electrophoretic mobility , which are recognized with high specificity by proteins HMG 1 and HMG 2 . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| RESULTS : Formation of Form 10 was found to occur upon reassociation of the strands of a DNA fragment containing a tract of poly ( CA ) . poly ( TG ) , in a process strongly stimulated by the nuclear proteins HMG 1 and HMG 2 . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| High affinity binding of proteins HMG 1 and HMG 2 to semicatenated DNA loops . ^^^ RESULTS : Here we show that HMG 1 and HMG 2 bind with a much higher affinity , at least 4 orders of magnitude higher , to a new structure , Form 10 , which consists of a DNA loop closed at its base by a semicatenated DNA junction , forming a DNA hemicatenane . ^^^ CONCLUSIONS : Of all DNA structures described so far with which HMG 1 and HMG 2 interact , we have found that Form 10 , a DNA loop with a semicatenated DNA junction at its base , is the structure with the highest affinity by more than 4 orders of magnitude . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| The high mobility group ( HMG ) proteins HMG 1 , HMG 2 and HMG2a are relatively abundant vertebrate DNA binding and bending proteins that bind with structure specificity , rather than sequence specificity , and appear to play an architectural role in the assembly of nucleoprotein complexes . ^^^ To gain insights into the role of the acidic tail , we examined the DNA binding properties of HMG 1 , HMG2b and HMG2a from chicken erythrocytes ( corresponding to HMG 1 , HMG 2 and HMG2a in other vertebrates ) . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Previous reports have shown that architectural DNA bending / looping chromosomal proteins HMGB 1 and HMGB 2 ( formerly known as HMG 1 and HMG 2 ) , which function in a number of biological processes including transcription and DNA repair , interact in vitro with p 53 and stimulate p 53 binding to DNA containing p 53 consensus sites . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Although the RAG proteins themselves bind and cleave DNA substrates containing either a 12 RSS or a 23 RSS , DNA bending proteins HMG 1 and HMG 2 are known to promote these processes , particularly with 23 RSS substrates . ^^^ Using in gel cleavage assays and DNA footprinting techniques , 1 analyzed the catalytic activity and protein DNA contacts in discrete 12 RSS and 23 RSS complexes containing the RAG proteins and either HMG 1 or HMG 2 . 1 found that both the cleavage activity and the pattern of protein DNA contacts in RAG HMG complexes assembled on 12 RSS substrates closely resembled those obtained from analogous 12 RSS complexes lacking HMG protein . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| This physical association suggests that HMG 2 may facilitate the nucleosome assembly , transcriptional activation , and DNA repair functions of SET and / or APE . ^^^ HMG 2 , like SET and APE , is a physiologically relevant granzyme A substrate in targeted cells . ^^^ Granzyme A cleavage and functional disruption of key nuclear substrates , including HMG 2 , SET , APE , lamins , and histones , are likely to cripple the cellular repair response to promote cell death in this novel caspase independent death pathway . . ^^^ We now find that the SET complex contains DNA binding and bending activities mediated by the chromatin associated protein HMG 2 . ^^^ HMG 2 facilitates assembly of nucleoprotein higher order structures by bending and looping DNA or by stabilizing underwound DNA . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| A GzmA activated DNase ( GAAD ) is in an ER associated complex containing pp 32 and the GzmA substrates SET , HMG 2 , and Ape 1 . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Limited proteolysis of a high molecular mass complex containing SET ( also named putative HLA associated protein 2 or PHAPII ) , PHAPI ( pp 32 , leucine rich acidic nuclear protein ) and HMG 2 by GzmA liberates NM 23 H1 , a Mg2+ dependent DNase that causes single stranded breaks in nuclear DNA . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| A special target of the granzyme A cell death pathway is an endoplasmic reticulum associated complex , called the SET complex , which contains three granzyme A substrates , the nucleosome assembly protein SET , the DNA bending protein HMG 2 , and the base excision repair endonuclease Ape 1 . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Synapsis of recombination signal sequences located in cis and DNA underwinding in 5 ( D ) J recombination . 5 ( D ) J recombination requires binding and synapsis of a complementary ( 12 / 23 ) pair of recombination signal sequences ( RSSs ) by the RAG 1 and RAG 2 proteins , aided by a high mobility group protein , HMG 1 or HMG 2 . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Involvement of HMGB 1 and HMGB 2 proteins in exogenous DNA integration reaction into the genome of HeLa S 3 cells . ^^^ These results indicate that HMGB 1 and HMGB 2 each have a novel function as stimulators of stable integration of plasmid DNA into the host genome and that they may be important for the process of spontaneous DNA integration in living cells . . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Dual binding modes for an HMG domain from human HMGB 2 on DNA . ^^^ In the presence of nanomolar concentrations of isolated HMG box A from HMGB 2 , DNA shows a decrease in its persistence length , where the protein induces an average DNA bend angle of 114 + / 21 degrees for 50 mM Na+ , and 87 + / 9 degrees for 100 mM Na+ . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Efficient assembly of RAG1 / 2 recombination signal sequence ( RSS ) DNA complexes that are competent for 5 ( D ) J cleavage requires the presence of the nonspecific DNA binding and bending protein HMGB 1 or HMGB 2 . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| Within this group , five genes ( GAPD , HMGB 2 , HSC 70 , GRP 58 , and HMGB 1 ) , previously shown to form a nuclear complex associated with resistance to DNA conformation altering chemotherapeutic drugs in in vitro systems , may represent a novel class of genes associated with in vivo drug response in ovarian cancer patients . ^^^ |
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| Interacting proteins: P26583 and P27695 |
Pubmed |
SVM Score :0.0 |
| In this analysis , 4 out of 5 members of the SET complex , SET , APE 1 , NM 23 and HMGB 2 , were highly expressed in invasive grade 3 tumors . ^^^ When combined , high expression of Hmgb 2 and low expression of Ape 1 was also associated with patient prognosis ( p = 0 . 05 ) . ^^^ |
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