期刊
EMBO JOURNAL
卷 19, 期 5, 页码 1148-1156出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.5.1148
关键词
DNA strand exchange; homologous recombination; joint molecule formation
资金
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI018987] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062653] Funding Source: NIH RePORTER
- NIAID NIH HHS [AI-18987] Funding Source: Medline
- NIGMS NIH HHS [R01 GM062653] Funding Source: Medline
The repair of potentially lethal DNA double-stranded breaks (DSBs) by homologous recombination requires processing of the broken DIVA into a resected DNA duplex with a protruding 3'-single-stranded DNA (ssDNA) tail. Accordingly, the canonical models for DSB repair require invasion of an intact homologous DNA template by the 3'-end of the ssDNA, a characteristic that the bacterial pairing protein RecA possesses. Unexpectedly, we find that for the eukaryotic homolog, Rad51 protein, the 5'-end of ssDNA is more invasive than the 3'-end. This pairing bias is unaffected by Rad52, Rad54 or Bad55-57 proteins. However, further investigation reveals that, in contrast to RecA protein, the preferred DNA substrate for Rad51 protein is not ssDNA but rather dsDNA with ssDNA tails. This important distinction permits the Rad51 proteins to promote DNA strand invasion using either 3'; or 5'-ends with similar efficiency.
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