The DOI matches its Crossref record.
Catalysis of ATP-Dependent Homologous DNA Pairing and Strand Exchange by Yeast RAD51 Protein
Abstract
The RAD51 gene of Saccharomyces cerevisiae is required for genetic recombination and DNA double-strand break repair. Here it is demonstrated that RAD51 protein pairs circular viral single-stranded DNA from φX 174 or M13 with its respective homologous linear double-stranded form. The product of synapsis between these DNA partners is further processed by RAD51 to yield nicked circular duplex DNA, which indicates that RAD51 can catalyze strand exchange. The pairing and strand exchange reaction requires adenosine triphosphate, a result consistent with the presence of a DNA-dependent adenosine triphosphatase activity in RAD51 protein. Thus, RAD51 is a eukaryotic recombination protein that can catalyze the strand exchange reaction.
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Research works printed but not linked: 19
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Cited by
Molecular Mechanisms of Mammalian DNA Repair and the DNA Damage Checkpoints
Sancar, A., Lindsey-Boltz, L. A., Ünsal-Kaçmaz, K., & Linn, S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073723 · Cited by 3,317
Multiple Pathways of Recombination Induced by Double-Strand Breaks in Saccharomyces cerevisiae
Pâques, F., & Haber, J. E. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.2.349-404.1999 · Cited by 2,120
Association of BRCA1 with Rad51 in Mitotic and Meiotic Cells
Scully, R., Chen, J., Plug, A., Xiao, Y., Weaver, D., Feunteun, J., Ashley, T., & Livingston, D. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81847-4 · Cited by 1,459
XRCC3 promotes homology-directed repair of DNA damage in mammalian cells
Pierce, A. J., Johnson, R. D., Thompson, L. H., & Jasin, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2633 · Cited by 1,379
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Metadata
- Authors
- Sung, P.
- Venue
- Science
- Published
- 1994-08-26
- Volume
- 265
- Issue
- 5176
- Pages
- 1241-1243
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2052521064
- Cited by
- 866
- References
- 0
- FWCI
- 15.20
- Type
- journal article
- Language
- en
- Open access
- closed
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