An OB-fold complex controls the repair pathways for DNA double-strand breaks

How repair pathway selection occurs is still a matter of debate and many factors have been associated to this function. Here the authors provide insight into the role of FAM35A and C20ORF196, two REV7-interacting proteins, which are recruited at double-strand breaks to promote non-homologous end joi...

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Main Authors:	Shengxian Gao, Sumin Feng, Shaokai Ning, Jingyan Liu, Huayu Zhao, Yixi Xu, Jinfeng Shang, Kejiao Li, Qing Li, Rong Guo, Dongyi Xu
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-09-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-06407-7

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spelling	doaj-55ad8f7d27a64b04b08dc7e043796b6b2021-05-11T10:17:30ZengNature Publishing GroupNature Communications2041-17232018-09-019111010.1038/s41467-018-06407-7An OB-fold complex controls the repair pathways for DNA double-strand breaksShengxian Gao0Sumin Feng1Shaokai Ning2Jingyan Liu3Huayu Zhao4Yixi Xu5Jinfeng Shang6Kejiao Li7Qing Li8Rong Guo9Dongyi Xu10State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking UniversityHow repair pathway selection occurs is still a matter of debate and many factors have been associated to this function. Here the authors provide insight into the role of FAM35A and C20ORF196, two REV7-interacting proteins, which are recruited at double-strand breaks to promote non-homologous end joining repair.https://doi.org/10.1038/s41467-018-06407-7
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Shengxian Gao Sumin Feng Shaokai Ning Jingyan Liu Huayu Zhao Yixi Xu Jinfeng Shang Kejiao Li Qing Li Rong Guo Dongyi Xu
spellingShingle	Shengxian Gao Sumin Feng Shaokai Ning Jingyan Liu Huayu Zhao Yixi Xu Jinfeng Shang Kejiao Li Qing Li Rong Guo Dongyi Xu An OB-fold complex controls the repair pathways for DNA double-strand breaks Nature Communications
author_facet	Shengxian Gao Sumin Feng Shaokai Ning Jingyan Liu Huayu Zhao Yixi Xu Jinfeng Shang Kejiao Li Qing Li Rong Guo Dongyi Xu
author_sort	Shengxian Gao
title	An OB-fold complex controls the repair pathways for DNA double-strand breaks
title_short	An OB-fold complex controls the repair pathways for DNA double-strand breaks
title_full	An OB-fold complex controls the repair pathways for DNA double-strand breaks
title_fullStr	An OB-fold complex controls the repair pathways for DNA double-strand breaks
title_full_unstemmed	An OB-fold complex controls the repair pathways for DNA double-strand breaks
title_sort	ob-fold complex controls the repair pathways for dna double-strand breaks
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-09-01
description	How repair pathway selection occurs is still a matter of debate and many factors have been associated to this function. Here the authors provide insight into the role of FAM35A and C20ORF196, two REV7-interacting proteins, which are recruited at double-strand breaks to promote non-homologous end joining repair.
url	https://doi.org/10.1038/s41467-018-06407-7
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An OB-fold complex controls the repair pathways for DNA double-strand breaks

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