Institute of Chemical Biology and Fundamental Medicine, Novosibirsk, Russia.
Department of Natural Sciences, Novosibirsk State University, Novosibirsk, Russia.
Photochem Photobiol. 2020 Mar;96(2):440-449. doi: 10.1111/php.13222. Epub 2020 Mar 5.
Replication protein A (RPA), eukaryotic single-stranded DNA-binding protein, is a key player in multiple processes of DNA metabolism including DNA replication, recombination and DNA repair. Human RPA composed of subunits of 70-, 32- and 14-kDa binds ssDNA with high affinity and interacts specifically with multiple proteins. The RPA heterotrimer binds ssDNA in several modes, with occlusion lengths of 8-10, 13-22 and 30 nucleotides corresponding to global, transitional and elongated conformations of protein. Varying the structure of photoreactive DNA, the intermediates of different stages of DNA replication or DNA repair were designed and applied to identify positioning of the RPA subunits on the specific DNA structures. Using this approach, RPA interactions with various types of DNA structures attributed to replication and DNA repair intermediates were examined. This review is dedicated to blessed memory of Prof. Alain Favre who contributed to the development of photoreactive nucleotide derivatives and their application for the study of protein-nucleic acids interactions.
复制蛋白 A（RPA）是一种真核单链 DNA 结合蛋白，是 DNA 代谢包括 DNA 复制、重组和 DNA 修复等多个过程中的关键参与者。由 70kDa、32kDa 和 14kDa 亚基组成的人源 RPA 与 ssDNA 具有高亲和力结合，并与多种蛋白质特异性相互作用。RPA 异三聚体以几种模式结合 ssDNA，8-10、13-22 和 30 个核苷酸的阻断长度分别对应于蛋白质的全局、过渡和延伸构象。通过改变光反应性 DNA 的结构，设计并应用不同阶段的 DNA 复制或 DNA 修复的中间体，以确定 RPA 亚基在特定 DNA 结构上的定位。使用这种方法，研究了 RPA 与各种类型的 DNA 结构的相互作用，这些结构归因于复制和 DNA 修复中间体。本文谨以此文纪念为光反应性核苷酸衍生物的发展及其在研究蛋白-核酸相互作用中的应用做出贡献的 Alain Favre 教授。
