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Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles

The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The inc...

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Autores principales: Wang, Weibin, Daley, James M., Kwon, Youngho, Krasner, Danielle S., Sung, Patrick
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795780/
https://www.ncbi.nlm.nih.gov/pubmed/29321177
http://dx.doi.org/10.1101/gad.307900.117
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author Wang, Weibin
Daley, James M.
Kwon, Youngho
Krasner, Danielle S.
Sung, Patrick
author_facet Wang, Weibin
Daley, James M.
Kwon, Youngho
Krasner, Danielle S.
Sung, Patrick
author_sort Wang, Weibin
collection PubMed
description The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery.
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spelling pubmed-57957802018-06-01 Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles Wang, Weibin Daley, James M. Kwon, Youngho Krasner, Danielle S. Sung, Patrick Genes Dev Research Communication The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery. Cold Spring Harbor Laboratory Press 2017-12-01 /pmc/articles/PMC5795780/ /pubmed/29321177 http://dx.doi.org/10.1101/gad.307900.117 Text en © 2018 Wang et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/4.0/ 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 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Research Communication
Wang, Weibin
Daley, James M.
Kwon, Youngho
Krasner, Danielle S.
Sung, Patrick
Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles
title Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles
title_full Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles
title_fullStr Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles
title_full_unstemmed Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles
title_short Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstacles
title_sort plasticity of the mre11–rad50–xrs2–sae2 nuclease ensemble in the processing of dna-bound obstacles
topic Research Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795780/
https://www.ncbi.nlm.nih.gov/pubmed/29321177
http://dx.doi.org/10.1101/gad.307900.117
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