期刊
FEBS OPEN BIO
卷 11, 期 3, 页码 622-632出版社
WILEY
DOI: 10.1002/2211-5463.13071
关键词
DNA repair; DNA‐ end resection; MRGBP; recombination; TIP60
资金
- R+D+I grant from the Spanish Ministry of Economy and Competitivity [SAF2016-74855-P]
- European Union Regional Funds (FEDER)
- Regional Government of Andalucia (Junta de Andalucia)
- program 'GARANTiA JUVENIL EN LA UNIVERSIDAD DE SEVILLA'
This study demonstrates that MRG domain binding protein (MRGBP) acts as a general inhibitor of DNA double-strand break repair, with its downregulation leading to an overall increase in repair, particularly in stimulating early events of homologous recombination.
The repair of DNA breaks takes place in the context of chromatin and thus involves the activity of chromatin remodelers. The nucleosome acetyltransferase of H4 (NuA4) remodeler complex enables DNA break repair by relaxing flanking chromatin. Here, we show that MRG domain binding protein (MRGBP), a member of this complex, acts as a general inhibitor of DNA double-strand break repair. Upon its downregulation, repair is generally increased. This is particularly evident for the stimulation of early events of homologous recombination. Thus, MRGBP has an opposing role to the main catalytic subunits of the NuA4 complex. Our data suggest that MRGBP acts by limiting the activity of this complex in DNA repair, specifically by narrowing the extent of DNA-end resection.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据