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首页> 外文期刊>Molecular and Cellular Biology >Functional interaction between p53, the TATA-binding protein (TBP), andTBP-associated factors in vivo.
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Functional interaction between p53, the TATA-binding protein (TBP), andTBP-associated factors in vivo.

机译：p53，TATA结合蛋白（TBP）和TBP相关因子在体内的功能相互作用。

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The transcriptional activator p53 is known to interact with components of the general transcription factor TFIID in vitro. To examine the relevance of these associations to transcriptional activation in vivo, plasmids expressing a p53-GAL4 chimera and Drosophila TATA-binding protein (dTBP) were transfected into Drosophila Schneider cells. p53-GAL4 and dTBP displayed a markedly synergistic effect on activated transcription from a GAL4 site-containing reporter that was at least 10-fold greater than observed with other activators tested. A mutant p53 previously shown to be defective in both transcriptional activation in vivo and in binding to TBP-associated factors (TAFs) in vitro, although still capable of binding dTBP, did not cooperate with dTBP, suggesting that TAFs may contribute to this synergy. Providing further support for this possibility, transfected dTBP assembled into rapidly sedimenting complexes and could be immunoprecipitated with anti-TAF antibodies. While overexpression of any of several TAFs did not affect basal transcription, in either the presence or the absence of cotransfected dTBP, overexpression of TAFII230 inhibited transcriptional activation mediated by p53-GAL4 as well as by GAL4-VP16 and Sp1. Overexpression of TAFII40 and TAFII60 also inhibited activation by p53-GAL4 but had negligible effects on activation by GAL4-VP16 and Sp1, while TAFII110 did not affect any of the activators. TAF-mediated inhibition of activated transcription could be rescued by high levels of exogenous dTBP, which also restored full synergy. These data demonstrate for the first time that functional interactions can occur in vivo between TBP, TAFs, and p53.
机译：已知转录激活因子p53在体外与一般转录因子TFIID的成分相互作用。为了检查这些关联与体内转录激活的相关性，将表达p53-GAL4嵌合体和果蝇TATA结合蛋白（dTBP）的质粒转染到果蝇施耐德细胞中。 p53-GAL4和dTBP对来自含GAL4位点的报道分子的活化转录显示出明显的协同作用，该效应至少比其他测试的活化剂高10倍。突变体p53先前在体内转录激活和体外与TBP相关因子（TAFs）结合方面均表现出缺陷，尽管它仍然能够结合dTBP，但并未与dTBP协同作用，表明TAF可能有助于这种协同作用。为这种可能性提供了进一步的支持，转染的dTBP组装成快速沉降的复合物，并可以用抗TAF抗体进行免疫沉淀。尽管在存在或不存在共转染的dTBP的情况下，几种TAF中的任何一种的过表达都不会影响基础转录，但是TAFII230的过表达抑制了p53-GAL4以及GAL4-VP16和Sp1介导的转录激活。 TAFII40和TAFII60的过表达也抑制了p53-GAL4的激活，但对GAL4-VP16和Sp1的激活的影响可忽略不计，而TAFII110不影响任何激活剂。 TAF介导的激活转录抑制可通过高水平的外源性dTBP挽救，这也恢复了完全的协同作用。这些数据首次证明了TBP，TAF和p53之间可以在体内发生功能性相互作用。

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