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首页> 外文期刊>Molecular and Cellular Biology >Detection of RAG Protein-V(D)J Recombination Signal Interactions Near the Site of DNA Cleavage by UV Cross-Linking
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Detection of RAG Protein-V(D)J Recombination Signal Interactions Near the Site of DNA Cleavage by UV Cross-Linking

机译：通过紫外交联检测DNA切割位点附近的RAG蛋白-V（D）J重组信号相互作用。

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摘要

V(D)J recombination is initiated by double-strand cleavage at recombination signal sequences (RSSs). DNA cleavage is mediated by the RAG1 and RAG2 proteins. Recent experiments describing RAG protein-RSS complexes, while defining the interaction of RAG1 with the nonamer, have not assigned contacts immediately adjacent to the site of DNA cleavage to either RAG polypeptide. Here we use UV cross-linking to define sequence- and site-specific interactions between RAG1 protein and both the heptamer element of the RSS and the coding flank DNA. Hence, RAG1-DNA contacts span the site of cleavage. We also detect cross-linking of RAG2 protein to some of the same nucleotides that cross-link to RAG1, indicating that, in the binding complex, both RAG proteins are in close proximity to the site of cleavage. These results suggest how the heptamer element, the recognition surface essential for DNA cleavage, is recognized by the RAG proteins and have implications for the stoichiometry and active site organization of the RAG1-RAG2-RSS complex.
机译：V（D）J重组是通过重组信号序列（RSSs）上的双链切割而启动的。 DNA切割是由RAG1和RAG2蛋白介导的。描述RAG蛋白-RSS复合物的最新实验，尽管定义了RAG1与九聚体的相互作用，但并未将与DNA切割位点紧邻的接触分配给任一RAG多肽。在这里，我们使用紫外线交联来定义RAG1蛋白与RSS的七聚体元件和编码侧翼DNA之间的序列和位点特异性相互作用。因此，RAG1-DNA接触跨越了切割位点。我们还检测到RAG2蛋白与一些交联到RAG1的相同核苷酸的交联，这表明在结合复合物中，两个RAG蛋白都非常靠近切割位点。这些结果表明，七聚体元件是DNA裂解必不可少的识别表面，如何被RAG蛋白识别，并影响RAG1-RAG2-RSS复合物的化学计量和活性位点组织。

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