Dual regulation of Dmc1-driven DNA strand exchange by Swi5-Sfr1 activation and Rad22 inhibition.
Dual regulation of Dmc1-driven DNA strand exchange by Swi5-Sfr1 activation and Rad22 inhibition.
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DOI：
10.1101/gad.218693.113
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发表时间：
2013-11-01
影响因子：
10.5
通讯作者：
Iwasaki H
中科院分区：
文献类型：
--
作者：
Murayama Y;Kurokawa Y;Tsutsui Y;Iwasaki H
Meiotic recombination requires two key recombinases: the ubiquitously expressed Rad51 and the meiosis-specific Dmc1. Rad52 and its fission yeast ortholog, Rad22, are mediators that help load Rad51 onto ssDNA coated with replication protein A (RPA). Here, Iwasaki and colleagues reveal how the Swi5–Sfr1 complex functions as both a mediator (loading DMC1 onto ssDNA) and an activator (stimulating Dmc1-driven strand exchange). In contrast, Rad22 inhibits Dmc1 by competing for binding to RPA-coated ssDNA. This study thus provides a novel regulatory mechanism for meiotic recombination. Both ubiquitously expressed Rad51 and meiosis-specific Dmc1 are required for crossover production during meiotic recombination. The budding yeast Rad52 and its fission yeast ortholog, Rad22, are “mediators;” i.e., they help load Rad51 onto ssDNA coated with replication protein A (RPA). Here we show that the Swi5–Sfr1 complex from fission yeast is both a mediator that loads Dmc1 onto ssDNA and a direct “activator” of DNA strand exchange by Dmc1. In stark contrast, Rad22 inhibits Dmc1 action by competing for its binding to RPA-coated ssDNA. Thus, Rad22 plays dual roles in regulating meiotic recombination: activating Rad51 and inhibiting Dmc1.
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