期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 11, 页码 1093-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2394
关键词
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资金
- Division of Signal Transduction Therapy Unit
- AstraZeneca
- Boehringer-Ingelheim
- GlaxoSmithKline
- Merck KgaA
- Janssen Pharmaceutica
- Pfizer
- Medical Research Council Protein Phosphorylation Unit
- Medical Research Council UK
- Association for International Cancer Research
- Cancer Research UK
- Cancer Research UK [11243] Funding Source: researchfish
- Medical Research Council [MC_U127070192] Funding Source: researchfish
- MRC [MC_U127070192] Funding Source: UKRI
Ubiquitin-binding domains (UBDs) are crucial for recruiting many proteins to sites of DNA damage. Here we characterize C1orf124 (Spartan; referred to as DVC1), which has an UBZ4-type UBD found predominantly in DNA repair proteins. DVC1 associates with DNA replication factories and localizes to sites of DNA damage in human cells, in a manner that requires the ability of the DVC1 UBZ domain to bind to ubiquitin polymers in vitro and a conserved PCNA-interacting motif. DVC1 interacts with the p97 protein 'segregase'. We show that DVC1 recruits p97 to sites of DNA damage, where we propose that p97 facilitates the extraction of the translesion synthesis (TLS) polymerase (Pol) eta during DNA repair to prevent excessive TLS and limit the incidence of mutations induced by DNA damage. We introduce DVC1 as a regulator of cellular responses to DNA damage that prevents mutations when DNA damage occurs.
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