Journal article
The RecA/RAD51 protein drives migration of Holliday junctions via polymerization on DNA
Proceedings of the National Academy of Sciences - PNAS, v 108(16), pp 6432-6437
19 Apr 2011
PMID: 21464277
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The Holliday junction (HJ), a cross-shaped structure that physically links the two DNA helices, is a key intermediate in homologous recombination, DNA repair, and replication. Several helicase-like proteins are known to bind HJs and promote their branch migration (BM) by translocating along DNA at the expense of ATP hydrolysis. Surprisingly, the bacterial recombinase protein RecA and its eukaryotic homologue Rad51 also promote BM of HJs despite the fact they do not bind HJs preferentially and do not translocate along DNA. RecA/Rad51 plays a key role in DNA double-stranded break repair and homologous recombination. RecA/Rad51 binds to ssDNA and forms contiguous filaments that promote the search for homologous DNA sequences and DNA strand exchange. The mechanism of BM promoted by RecA/RAD51 is unknown. Here, we demonstrate that cycles of RecA/Rad51 polymerization and dissociation coupled with ATP hydrolysis drives the BM of HJs.
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Details
- Title
- The RecA/RAD51 protein drives migration of Holliday junctions via polymerization on DNA
- Creators
- Matthew J Rossi - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102-1192; andOlga M Mazina - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102-1192; andDmitry V Bugreev - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102-1192; andAlexander V Mazin - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102-1192; and
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 108(16), pp 6432-6437
- Publisher
- National Academy of Sciences
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000289680400026
- Scopus ID
- 2-s2.0-79955632936
- Other Identifier
- 991014878273204721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology