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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >THE ABILITY TO ASSOCIATE WITH ACTIVATION DOMAINS IN VITRO IS NOT REQUIRED FOR THE TATA BOX-BINDING PROTEIN TO SUPPORT ACTIVATED TRANSCRIPTION IN VIVO
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THE ABILITY TO ASSOCIATE WITH ACTIVATION DOMAINS IN VITRO IS NOT REQUIRED FOR THE TATA BOX-BINDING PROTEIN TO SUPPORT ACTIVATED TRANSCRIPTION IN VIVO

机译：TATA盒结合蛋白支持活体内转录的激活并不需要与激活域进行体外关联

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摘要

The TATA box-binding protein (TBP) interacts in vitro with the activation domains of many viral and cellular transcription factors and has been proposed to be a direct target for transcriptional activators. We have examined the functional relevance of activator-TBP association in vitro to transcriptional activation in vivo. We show that alanine substitution mutations in a single loop of TBP can disrupt its association in vitro with the activation domains of the herpes simplex virus activator VP16 and of the human tumor suppressor protein p53; these mutations do not, however, disrupt the transcriptional response of TBP to either activation domain in vivo. Moreover, we show that a region of VP16 distinct from its activation domain can also tightly associate with TBP in vitro, but fails to activate transcription in vivo. These data suggest that the ability of TBP to interact with activation domains in vitro is not directly relevant to its ability to support activated transcription in vivo. [References: 39]
机译：TATA盒结合蛋白（TBP）在体外与许多病毒和细胞转录因子的激活域相互作用，并已被提出是转录激活因子的直接靶标。我们已经检查了激活剂-TBP关联在体外与体内转录激活的功能相关性。我们显示，TBP的单个环中的丙氨酸取代突变可以在体外破坏与单纯疱疹病毒激活剂VP16和人类肿瘤抑制蛋白p53的激活域的关联；然而，这些突变不会破坏TBP对体内任一激活域的转录反应。此外，我们表明，不同于其激活结构域的VP16区域也可以在体外与TBP紧密结合，但不能在体内激活转录。这些数据表明，TBP在体外与激活域相互作用的能力与其在体内支持激活转录的能力没有直接关系。 [参考：39]

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