RPA interacts with Rad52 to promote meiotic crossover and noncrossover recombination.

Autor:	Joo JH; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea., Hong S; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea., Higashide MT; Institute for Protein Research, Graduate School of Science, Osaka University, Osaka 565-0871, Japan., Choi EH; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea.; New Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Deagu 41061, South Korea., Yoon S; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea., Lee MS; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea., Kang HA; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea., Shinohara A; Institute for Protein Research, Graduate School of Science, Osaka University, Osaka 565-0871, Japan., Kleckner N; Department of Molecular and Cellular Biology, Harvard University, Cambridge 02138, USA., Kim KP; Department of Life Sciences, Chung-Ang University, Seoul 06974, South Korea.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2024 Apr 24; Vol. 52 (7), pp. 3794-3809.
DOI:	10.1093/nar/gkae083
Abstrakt:	Meiotic recombination is initiated by programmed double-strand breaks (DSBs). Studies in Saccharomyces cerevisiae have shown that, following rapid resection to generate 3' single-stranded DNA (ssDNA) tails, one DSB end engages a homolog partner chromatid and is extended by DNA synthesis, whereas the other end remains associated with its sister. Then, after regulated differentiation into crossover- and noncrossover-fated types, the second DSB end participates in the reaction by strand annealing with the extended first end, along both pathways. This second-end capture is dependent on Rad52, presumably via its known capacity to anneal two ssDNAs. Here, using physical analysis of DNA recombination, we demonstrate that this process is dependent on direct interaction of Rad52 with the ssDNA binding protein, replication protein A (RPA). Furthermore, the absence of this Rad52-RPA joint activity results in a cytologically-prominent RPA spike, which emerges from the homolog axes at sites of crossovers during the pachytene stage of the meiotic prophase. Our findings suggest that this spike represents the DSB end of a broken chromatid caused by either the displaced leading DSB end or the second DSB end, which has been unable to engage with the partner homolog-associated ssDNA. These and other results imply a close correspondence between Rad52-RPA roles in meiotic recombination and mitotic DSB repair. (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Databáze:	MEDLINE
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