期刊
EMBO JOURNAL
卷 32, 期 1, 页码 126-139出版社
WILEY
DOI: 10.1038/emboj.2012.314
关键词
DNA repair; resection; RPA; single-stranded DNA
资金
- National Institutes of Health [CA094008, GM100196, RR025341, GM065367]
- National Science Foundation [0822613]
- CDMRP [W81XWH-09-1-0041]
- Cancer Prevention and Research. Institute of Texas [RP110465]
The human SSB homologue 1 (hSSB1) has been shown to facilitate homologous recombination and double-strand break signalling in human cells. Here, we compare the DNA-binding properties of the SOSS1 complex, containing SSB1, with Replication Protein A (RPA), the primary single-strand DNA (ssDNA) binding complex in eukaryotes. Ensemble and single-molecule approaches show that SOSS1 binds ssDNA with lower affinity compared to RPA, and exhibits less stable interactions with DNA substrates. Nevertheless, the SOSS1 complex is uniquely capable of promoting interaction of human Exo1 with double-strand DNA ends and stimulates its activity independently of the MRN complex in vitro. Both MRN and SOSS1 also act to mitigate the inhibitory action of the Ku70/80 heterodimer on Exo1 activity in vitro. These results may explain why SOSS complexes do not localize with RPA to replication sites in human cells, yet have a strong effect on double-strand break resection and homologous recombination. The EMBO Journal (2013) 32, 126-139. doi:10.1038/emboj.2012.314; Published online 23 November 2012
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