Journal article
Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing
The EMBO journal, v 19(5), pp 1148-1156
01 Mar 2000
PMID: 10698955
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The repair of potentially lethal DNA double-stranded breaks (DSBs) by homologous recombination requires processing of the broken DNA 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 Rad55–57 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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Details
- Title
- Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing
- Creators
- Alexander V Mazin - Division of Biological Sciences, Sections of Microbiology and of Molecular and Cellular Biology, University of California, Davis, CA 95616–8665 andElena Zaitseva - Division of Biological Sciences, Sections of Microbiology and of Molecular and Cellular Biology, University of California, Davis, CA 95616–8665 andPatrick Sung - Division of Biological Sciences, Sections of Microbiology and of Molecular and Cellular Biology, University of California, Davis, CA 95616–8665 andStephen C Kowalczykowski - Division of Biological Sciences, Sections of Microbiology and of Molecular and Cellular Biology, University of California, Davis, CA 95616–8665 and
- Publication Details
- The EMBO journal, v 19(5), pp 1148-1156
- Publisher
- Oxford University Press; Oxford, UK
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000085749600035
- Scopus ID
- 2-s2.0-0034161571
- Other Identifier
- 991014878186904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology