Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking

Michele A. Cleary; P. Shannon Pendergrast; Winship Herr

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Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking

机译：蛋白质-DNA光交联揭示了转录复合物形成中的结构灵活性

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The Oct-1 POU domain binds diverse DNA- sequence elements and forms a higher-order regulatory com- plex with the herpes simplex virus coregulator VP16. The POU domain contains two separate DNA-binding domains joined by a flexible linker. By protein-DNA photocrosslinking we show that the relative positioning of the two POU DNA- binding domains on DNA varies depending on the nature of the DNA target. On a single VP16-responsive element, the POU domain adopts multiple conformations. To determine the structure of the Oct-1 POU domain in a multiprotein complex with VP16, we allowed VP16 to interact with previ- ously crosslinked POU-domain-DNA complexes and found that VP16 can associate with multiple POU-domain confor- mations. These results reveal the dynamic potential of a DNA-binding domain in directing transcriptional regulatory complex formation.

机译：Oct-1 POU结构域结合了各种DNA序列元件，并与单纯疱疹病毒核心调节剂VP16形成了更高阶的调节复合物。 POU结构域包含两个单独的DNA结合结构域，通过柔性接头连接。通过蛋白质-DNA光交联，我们显示了两个POU DNA结合域在DNA上的相对位置根据DNA靶的性质而变化。在单个VP16响应元素上，POU域采用多种构型。为了确定带有VP16的多蛋白复合物中Oct-1 POU域的结构，我们允许VP16与先前交联的POU域-DNA复合物相互作用，并发现VP16可以与多个POU域构象结合。这些结果揭示了DNA结合域在指导转录调节复合物形成中的动态潜力。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1997年第16期|p.8450-8455|共6页
作者
Michele A. Cleary; P. Shannon Pendergrast; Winship Herr;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking

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