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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2017
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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. |
format | Online Article Text |
id | pubmed-5795780 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
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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