蛋白质-DNA光交联揭示转录复合物形成过程中的结构灵活性
Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking.
作者信息
Cleary M A, Pendergrast P S, Herr W
机构信息
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
出版信息
Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8450-5. doi: 10.1073/pnas.94.16.8450.
Abstract
The Oct-1 POU domain binds diverse DNA-sequence elements and forms a higher-order regulatory complex 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 previously crosslinked POU-domain-DNA complexes and found that VP16 can associate with multiple POU-domain conformations. These results reveal the dynamic potential of a DNA-binding domain in directing transcriptional regulatory complex formation.
摘要
Oct-1 POU结构域可结合多种DNA序列元件，并与单纯疱疹病毒共调节因子VP16形成高级调控复合物。POU结构域包含两个由柔性接头连接的独立DNA结合结构域。通过蛋白质-DNA光交联，我们发现两个POU DNA结合结构域在DNA上的相对定位因DNA靶标的性质而异。在单个VP16反应元件上，POU结构域呈现多种构象。为了确定Oct-1 POU结构域在与VP16形成的多蛋白复合物中的结构，我们让VP16与先前交联的POU结构域-DNA复合物相互作用，发现VP16可以与多种POU结构域构象结合。这些结果揭示了DNA结合结构域在指导转录调控复合物形成中的动态潜力。
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