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Role of the Rad52 amino-terminal DNA binding activity in DNA strand capture in homologous recombination.
J Biol Chem. 2009 Nov 27; 284(48):33275-84.JB

Abstract

Saccharomyces cerevisiae Rad52 protein promotes homologous recombination by nucleating the Rad51 recombinase onto replication protein A-coated single-stranded DNA strands and also by directly annealing such strands. We show that the purified rad52-R70A mutant protein, with a compromised amino-terminal DNA binding domain, is capable of Rad51 delivery to DNA but is deficient in DNA annealing. Results from chromatin immunoprecipitation experiments find that rad52-R70A associates with DNA double-strand breaks and promotes recruitment of Rad51 as efficiently as wild-type Rad52. Analysis of gene conversion intermediates reveals that rad52-R70A cells can mediate DNA strand invasion but are unable to complete the recombination event. These results provide evidence that DNA binding by the evolutionarily conserved amino terminus of Rad52 is needed for the capture of the second DNA end during homologous recombination.

Authors+Show Affiliations

Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19812039

Citation

Shi, Idina, et al. "Role of the Rad52 Amino-terminal DNA Binding Activity in DNA Strand Capture in Homologous Recombination." The Journal of Biological Chemistry, vol. 284, no. 48, 2009, pp. 33275-84.
Shi I, Hallwyl SC, Seong C, et al. Role of the Rad52 amino-terminal DNA binding activity in DNA strand capture in homologous recombination. J Biol Chem. 2009;284(48):33275-84.
Shi, I., Hallwyl, S. C., Seong, C., Mortensen, U., Rothstein, R., & Sung, P. (2009). Role of the Rad52 amino-terminal DNA binding activity in DNA strand capture in homologous recombination. The Journal of Biological Chemistry, 284(48), 33275-84. https://doi.org/10.1074/jbc.M109.057752
Shi I, et al. Role of the Rad52 Amino-terminal DNA Binding Activity in DNA Strand Capture in Homologous Recombination. J Biol Chem. 2009 Nov 27;284(48):33275-84. PubMed PMID: 19812039.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of the Rad52 amino-terminal DNA binding activity in DNA strand capture in homologous recombination. AU - Shi,Idina, AU - Hallwyl,Swee C L, AU - Seong,Changhyun, AU - Mortensen,Uffe, AU - Rothstein,Rodney, AU - Sung,Patrick, Y1 - 2009/10/06/ PY - 2009/10/9/entrez PY - 2009/10/9/pubmed PY - 2010/1/22/medline SP - 33275 EP - 84 JF - The Journal of biological chemistry JO - J Biol Chem VL - 284 IS - 48 N2 - Saccharomyces cerevisiae Rad52 protein promotes homologous recombination by nucleating the Rad51 recombinase onto replication protein A-coated single-stranded DNA strands and also by directly annealing such strands. We show that the purified rad52-R70A mutant protein, with a compromised amino-terminal DNA binding domain, is capable of Rad51 delivery to DNA but is deficient in DNA annealing. Results from chromatin immunoprecipitation experiments find that rad52-R70A associates with DNA double-strand breaks and promotes recruitment of Rad51 as efficiently as wild-type Rad52. Analysis of gene conversion intermediates reveals that rad52-R70A cells can mediate DNA strand invasion but are unable to complete the recombination event. These results provide evidence that DNA binding by the evolutionarily conserved amino terminus of Rad52 is needed for the capture of the second DNA end during homologous recombination. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/19812039/Role_of_the_Rad52_amino_terminal_DNA_binding_activity_in_DNA_strand_capture_in_homologous_recombination_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)37764-4 DB - PRIME DP - Unbound Medicine ER -