Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition

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...

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Autores principales: Murayama, Yasuto, Kurokawa, Yumiko, Tsutsui, Yasuhiro, Iwasaki, Hiroshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2013
Materias:
Research Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828516/
https://www.ncbi.nlm.nih.gov/pubmed/24186976
http://dx.doi.org/10.1101/gad.218693.113
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author Murayama, Yasuto
Kurokawa, Yumiko
Tsutsui, Yasuhiro
Iwasaki, Hiroshi
author_facet Murayama, Yasuto
Kurokawa, Yumiko
Tsutsui, Yasuhiro
Iwasaki, Hiroshi
author_sort Murayama, Yasuto
collection PubMed
description 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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spelling pubmed-38285162014-05-01 Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition Murayama, Yasuto Kurokawa, Yumiko Tsutsui, Yasuhiro Iwasaki, Hiroshi Genes Dev Research Communication 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. Cold Spring Harbor Laboratory Press 2013-11-01 /pmc/articles/PMC3828516/ /pubmed/24186976 http://dx.doi.org/10.1101/gad.218693.113 Text en © 2013 Murayama et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.
spellingShingle Research Communication
Murayama, Yasuto
Kurokawa, Yumiko
Tsutsui, Yasuhiro
Iwasaki, Hiroshi
Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition
title Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition
title_full Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition
title_fullStr Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition
title_full_unstemmed Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition
title_short Dual regulation of Dmc1-driven DNA strand exchange by Swi5–Sfr1 activation and Rad22 inhibition
title_sort dual regulation of dmc1-driven dna strand exchange by swi5–sfr1 activation and rad22 inhibition
topic Research Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828516/
https://www.ncbi.nlm.nih.gov/pubmed/24186976
http://dx.doi.org/10.1101/gad.218693.113
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