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Title: Role of teh Rad52 Amino-terminal DNA Binding Activity in DNA Strand Capture in Homologous Recombination
Type: Journal articleJournal article
Participant(s):
Forfatter:  Shi, Idina
Yale University Scool of Medicine, Department of Molecular Biophysics and Biochemistry

Author:  Hallwyl, Swee Chuang Lim (Cwisno: 16944)
Technical University of Denmark

Forfatter:  Seong, Changhyun
Yale University Scool of Medicine, Department of Molecular Biophysics and Biochemistry

Author:  Mortensen, Uffe Hasbro (Cwisno: 7241)
Technical University of Denmark
Email:

Forfatter:  Rothstein, Rodney
Columbia University Medical Center, Department of Genetics and Development

Forfatter:  Sung, Patrick
Yale University Scool of Medicine, Department of Molecular Biophysics and Biochemistry
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.
Published: in journal: Journal of Biological Chemistry (ISSN: 0021-9258) (DOI: http://dx.doi.org/10.1074/jbc.M109.057752), vol: 284, issue: 48, pages: 33275-33284, 2009
DOI:
See the publication in DTU Orbit See the publication in DTU Orbit

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