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| Content Provider | PubMed Central |
|---|---|
| Author | Zeng, Ming Ren, Laifeng Mizuno, Ken'ichi Konstantinos, Nestoras Wang, Haibin Tang, Zizhi Guo, Liandi Kong, Daochun Hu, Qiwen He, Qun Du, Lilin Carr, Antony M. Liu, Cong |
| Copyright Year | 2016 |
| Abstract | Double-strand breaks repaired by homologous recombination (HR) are first resected to form single-stranded DNA, which binds replication protein A (RPA). RPA attracts mediators that load the Rad51 filament to promote strand invasion, the defining feature of HR. How the resection machinery navigates nucleosome-packaged DNA is poorly understood. Here we report that in Schizosaccharomyces pombe a conserved DDB1-CUL4-associated factor (DCAF), Wdr70, is recruited to DSBs as part of the Cullin4-DDB1 ubiquitin ligase (CRL4Wdr70) and stimulates distal H2B lysine 119 mono-ubiquitination (uH2B). Wdr70 deletion, or uH2B loss, results in increased loading of the checkpoint adaptor and resection inhibitor Crb253BP1, decreased Exo1 association and delayed resection. Wdr70 is dispensable for resection upon Crb253BP1 loss, or when the Set9 methyltransferase that creates docking sites for Crb2 is deleted. Finally, we establish that this histone regulatory cascade similarly controls DSB resection in human cells. |
| Related Links | http://dx.doi.org/10.1038/ncomms11364 |
| Starting Page | 11364 |
| File Format | |
| ISSN | 20411723 |
| e-ISSN | 20411723 |
| Journal | Nature Communications |
| Volume Number | 7 |
| Language | English |
| Publisher | Nature Publishing Group |
| Publisher Date | 2016-04-01 |
| Access Restriction | Open |
| Rights Holder | Nature Publishing Group |
| Subject Keyword | Biochemistry, Genetics and Molecular Biology(all) Physics and Astronomy(all) Chemistry(all) Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Chemistry Physics and Astronomy Biochemistry, Genetics and Molecular Biology |
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