| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.55319659 |
| Our results suggest a complex interaction between Rb and TAF ( 2 ) 250 and imply that TAF ( 2 ) 250 , TFIID , and potentially other basal transcription factors are targets for regulation by Rb and Rb related proteins . . 0.55319659^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.8998969 |
| We have demonstrated that recombinant Rb can compete with TBP and the p 62 subunit of TFIIH for binding to immobilized E2F1 . 0.8998969^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| These results suggest that RB can confer transcriptional regulation and possibly cell cycle control and tumor suppression through an interaction with TFIID , in particular with TAFII250 . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| To study the functional role of these interactions , we examined the properties of cellular retinoblastoma binding protein 2 ( RBP 2 ) binding to RB , p 107 , and the related TATA binding protein ( TBP ) product . ^^^ We observed that although RBP 2 bound exclusively to the T / E1A pocket of p 107 , it could interact with RB through independent T / E1A and non T / E1A domains and with TBP only through the non T / E1A domain . ^^^ Consistent with this observation , we found that a mutation within the Leu 10 Cys 10 Glu motif of RBP 2 resulted in loss of ability to precipitate p 107 , while RB and TBP binding activities were retained . ^^^ We located the non T / E1A binding site of RBP 2 on a 15 kDa fragment that is independent from the Leu 10 Cys 10 Glu motif and encodes binding activity for RB and TBP but does not interact with p 107 . ^^^ These findings confirm the differential binding specificities of the related RB , p 107 , and TBP proteins and support the presence of multifunctional domains on the nuclear RBP 2 product which may allow complex interactions with the cellular transcription machinery . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| Thirdly , the IE 2 domain required for RB binding is separate to the domains necessary for TBP and TFIIB binding . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| In this report , we show that when IE 2 86 is expressed as a glutathione S transferase ( GST ) IE 2 86 fusion protein , there are three independent regions that can interact with TBP and with another important cellular regulatory protein , the retinoblastoma gene product ( RB ) . ^^^ One of these three regions , as well as a domain at the carboxy terminus , contain consensus sites for casein kinase phosphorylation and negatively regulate binding of in vitro translated IE 2 86 to GST TBP or GST RB . ^^^ The dimerization domain of IE 2 86 must be present for the interaction of the in vitro translated protein with GST TBP and GST RB . ^^^ Our results also indicate that domains other than those that interact with TBP and RB are required for the activation function of this protein . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| Essentially the same region of the c Myc protein also binds the product of the retinoblastoma gene , the RB protein . c Myc protein coimmunoprecipitates with TBP in lysates of mammalian cells , demonstrating that the proteins are also complexed in vivo . ^^^ A short peptide that spans the RB binding site of the E 7 protein of human papilloma virus type 16 interferes with the binding of c Myc to TBP . ^^^ The same peptide also blocks binding of adenovirus E1A protein to TBP , suggesting that c Myc and E1A bind to RB and TBP through overlapping epitopes . ^^^ Furthermore , we show that binding of RB to E1A prevents association of E1A with TBP . ^^^ Our data suggest that one of the functions of RB and RB like proteins is to prevent interaction of viral and cellular oncoproteins , such as c Myc and E1A , with TBP . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| Consistent with this model , we find that the TATA box binding protein TBP can bind to the E2F activation domain in vitro in a manner indistinguishable from that of RB . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| The retinoblastoma ( RB ) tumor suppressor protein and the TATA box binding protein TFIID form contacts with a number of viral transactivator proteins . ^^^ The activation domain of transcription factor PU . 1 binds the retinoblastoma ( RB ) protein and the transcription factor TFIID in vitro : RB shows sequence similarity to TFIID and TFIIB . ^^^ Here we present evidence that the cellular transcription factor PU . 1 can bind to both RB and TFIID . ^^^ Like E1A , PU . 1 binds to the conserved C terminal domain of TFIID and to the RB `` pocket ' ' domain . ^^^ The ability of PU . 1 to contact directly both RB and TFIID through the same 75 residue domain prompted us to look for sequence similarity between these two proteins . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| We show that RB itself contains regions of homology to both TBP and BRF and propose a model in which RB disrupts TFIIIB by mimicking these two components . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| This is exemplified by the utilization of TBP as a component of SL 1 and the role of Rb in regulatory rDNA transcription . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| Since the TATA binding protein ( TBP ) is an important component for transcription mediated by all three RNA polymerases , we have analysed the functional interaction between Rb and TBP in vivo in the context of RNA pol 2 driven transcription . ^^^ We demonstrated that in mammalian cells Rb tethered to promoter represses TBP mediated activation in vivo , and Rb mediated repression is reversed in the presence of the inhibition of histone deacetylase activity by trichostatin A ( TSA ) . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| Here we report that the partial homeodomain binds the TATA binding protein ( TBP ) and retinoblastoma ( Rb ) gene product . ^^^ Both TBP and Rb were shown by coimmunoprecipitation experiments to directly associate with Pax 5 in vivo . ^^^ The conserved core domain of TBP and the pocket region as well as COOH terminal sequences of Rb are required for interaction with the partial homeodomain of Pax 5 in in vitro binding assays . ^^^ These data indicate that Pax 5 is able to contact the basal transcription machinery through the TBP containing initiation factor TFIID , and that its activity can be controlled by the cell cycle regulated association with Rb . . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| Here we demonstrate that the general transcription factors snRNA activating protein complex ( SNAP ( c ) ) and TATA binding protein ( TBP ) are important for RB repression of human U 6 snRNA gene transcription by RNA polymerase 3 . ^^^ TBP or a combination of TBP and SNAP ( c ) restores efficient U 6 transcription from RB treated extracts , indicating that TBP is also involved in RB regulation . ^^^ In contrast , the TBP containing complex TFIIIB restores adenovirus VAI but not human U 6 transcription in RB treated extracts , suggesting that TFIIIB is important for RB regulation of tRNA like genes . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| The interaction of regulatory transcription factors with RB may be explained by sequence similarity between RB and two general transcription factors : TBP and TFIIB . ^^^ |
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| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06400 and P20226 |
Pubmed |
SVM Score :0.0 |
| NA |
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