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Synergistic actions of Rad51 and Rad52 in recombination and DNA repair.
Nature. 1998 Jan 22; 391(6665):401-4.Nat

Abstract

In the yeast Saccharomyces cerevisiae, mutations in the genes RAD51 or RAD52 result in severe defects in genetic recombination and the repair of double-strand DNA breaks. These genes, and others of the RAD52 epistasis group (RAD50, RAD54, RAD55, RAD57, RAD59, MRE11 and XRS2), were first identified by their sensitivity to X-rays. They were subsequently shown to be required for spontaneous and induced mitotic recombination, meiotic recombination, and mating-type switching. Human homologues of RAD50, RAD51, RAD52, RAD54 and MRE11 have been identified. Targeted disruption of the murine RAD51 gene results in an embryonic lethal phenotype, indicating that Rad51 protein is required during cell proliferation. Biochemical studies have shown that human RAD51 encodes a protein of relative molecular mass 36,966 (hRad51) that promotes ATP-dependent homologous pairing and DNA strand exchange. As a structural and functional homologue of the RecA protein from Escherichia coli, hRad51 is thought to play a central role in recombination. Yeast Rad51 has been shown to interact with Rad52 protein, as does the human homologue. Here we show that hRad52 stimulates homologous pairing by hRad51. The DNA-binding properties of hRad52 indicate that Rad52 is involved in an early stage of Rad51-mediated recombination.

Authors+Show Affiliations

Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire, UK.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9450758

Citation

Benson, F E., et al. "Synergistic Actions of Rad51 and Rad52 in Recombination and DNA Repair." Nature, vol. 391, no. 6665, 1998, pp. 401-4.
Benson FE, Baumann P, West SC. Synergistic actions of Rad51 and Rad52 in recombination and DNA repair. Nature. 1998;391(6665):401-4.
Benson, F. E., Baumann, P., & West, S. C. (1998). Synergistic actions of Rad51 and Rad52 in recombination and DNA repair. Nature, 391(6665), 401-4.
Benson FE, Baumann P, West SC. Synergistic Actions of Rad51 and Rad52 in Recombination and DNA Repair. Nature. 1998 Jan 22;391(6665):401-4. PubMed PMID: 9450758.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Synergistic actions of Rad51 and Rad52 in recombination and DNA repair. AU - Benson,F E, AU - Baumann,P, AU - West,S C, PY - 1998/2/5/pubmed PY - 2001/3/23/medline PY - 1998/2/5/entrez SP - 401 EP - 4 JF - Nature JO - Nature VL - 391 IS - 6665 N2 - In the yeast Saccharomyces cerevisiae, mutations in the genes RAD51 or RAD52 result in severe defects in genetic recombination and the repair of double-strand DNA breaks. These genes, and others of the RAD52 epistasis group (RAD50, RAD54, RAD55, RAD57, RAD59, MRE11 and XRS2), were first identified by their sensitivity to X-rays. They were subsequently shown to be required for spontaneous and induced mitotic recombination, meiotic recombination, and mating-type switching. Human homologues of RAD50, RAD51, RAD52, RAD54 and MRE11 have been identified. Targeted disruption of the murine RAD51 gene results in an embryonic lethal phenotype, indicating that Rad51 protein is required during cell proliferation. Biochemical studies have shown that human RAD51 encodes a protein of relative molecular mass 36,966 (hRad51) that promotes ATP-dependent homologous pairing and DNA strand exchange. As a structural and functional homologue of the RecA protein from Escherichia coli, hRad51 is thought to play a central role in recombination. Yeast Rad51 has been shown to interact with Rad52 protein, as does the human homologue. Here we show that hRad52 stimulates homologous pairing by hRad51. The DNA-binding properties of hRad52 indicate that Rad52 is involved in an early stage of Rad51-mediated recombination. SN - 0028-0836 UR - https://www.unboundmedicine.com/medline/citation/9450758/Synergistic_actions_of_Rad51_and_Rad52_in_recombination_and_DNA_repair_ L2 - https://doi.org/10.1038/34937 DB - PRIME DP - Unbound Medicine ER -