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Keeping it real: MRX–Sae2 clipping of natural substrates

The yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together to initiate DNA end resection, an essential early step in homology-dependent repair of DNA double-strand breaks (DSBs). In this issue of Genes & Development, Wang and colleagues (pp. 2331–2336) and Reginato and colleagues (pp. 2...

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Detalles Bibliográficos
Autores principales: Gnügge, Robert, Symington, Lorraine S.
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/PMC5795777/
https://www.ncbi.nlm.nih.gov/pubmed/29352017
http://dx.doi.org/10.1101/gad.310771.117
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author Gnügge, Robert
Symington, Lorraine S.
author_facet Gnügge, Robert
Symington, Lorraine S.
author_sort Gnügge, Robert
collection PubMed
description The yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together to initiate DNA end resection, an essential early step in homology-dependent repair of DNA double-strand breaks (DSBs). In this issue of Genes & Development, Wang and colleagues (pp. 2331–2336) and Reginato and colleagues (pp. 2325–2330) report that a variety of physiological protein blocks, including Ku, RPA, and nucleosomes, stimulate MRX–Sae2 endonuclease cleavage in vitro. These studies have important implications for how cells deal with a range of barriers to end resection and highlight the crucial role of Sae2 in activating MRX cleavage at the correct cell cycle stage.
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spelling pubmed-57957772018-06-01 Keeping it real: MRX–Sae2 clipping of natural substrates Gnügge, Robert Symington, Lorraine S. Genes Dev Outlook The yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together to initiate DNA end resection, an essential early step in homology-dependent repair of DNA double-strand breaks (DSBs). In this issue of Genes & Development, Wang and colleagues (pp. 2331–2336) and Reginato and colleagues (pp. 2325–2330) report that a variety of physiological protein blocks, including Ku, RPA, and nucleosomes, stimulate MRX–Sae2 endonuclease cleavage in vitro. These studies have important implications for how cells deal with a range of barriers to end resection and highlight the crucial role of Sae2 in activating MRX cleavage at the correct cell cycle stage. Cold Spring Harbor Laboratory Press 2017-12-01 /pmc/articles/PMC5795777/ /pubmed/29352017 http://dx.doi.org/10.1101/gad.310771.117 Text en © 2018 Gnügge and Symington; 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 Outlook
Gnügge, Robert
Symington, Lorraine S.
Keeping it real: MRX–Sae2 clipping of natural substrates
title Keeping it real: MRX–Sae2 clipping of natural substrates
title_full Keeping it real: MRX–Sae2 clipping of natural substrates
title_fullStr Keeping it real: MRX–Sae2 clipping of natural substrates
title_full_unstemmed Keeping it real: MRX–Sae2 clipping of natural substrates
title_short Keeping it real: MRX–Sae2 clipping of natural substrates
title_sort keeping it real: mrx–sae2 clipping of natural substrates
topic Outlook
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5795777/
https://www.ncbi.nlm.nih.gov/pubmed/29352017
http://dx.doi.org/10.1101/gad.310771.117
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