Journal article
RSC Facilitates Rad59-Dependent Homologous Recombination between Sister Chromatids by Promoting Cohesin Loading at DNA Double-Strand Breaks
Molecular and cellular biology, Vol.31(19), pp.3924-3937
10/2011
DOI: 10.1128/MCB.01269-10
PMCID: PMC3187356
PMID: 21807899
Abstract
Homologous recombination repairs DNA double-strand breaks by searching for, invading, and copying information from a homologous template, typically the homologous chromosome or sister chromatid. Tight wrapping of DNA around histone octamers, however, impedes access of repair proteins to DNA damage. To facilitate DNA repair, modifications of histones and energy-dependent remodeling of chromatin are required, but the precise mechanisms by which chromatin modification and remodeling enzymes contribute to homologous DNA repair are unknown. Here we have systematically assessed the role of budding yeast RSC (remodel structure of chromatin), an abundant, ATP-dependent chromatin-remodeling complex, in the cellular response to spontaneous and induced DNA damage. RSC physically interacts with the recombination protein Rad59 and functions in homologous recombination. Multiple recombination assays revealed that RSC is uniquely required for recombination between sister chromatids by virtue of its ability to recruit cohesin at DNA breaks and thereby promoting sister chromatid cohesion. This study provides molecular insights into how chromatin remodeling contributes to DNA repair and maintenance of chromatin fidelity in the face of DNA damage.
Details
- Title: Subtitle
- RSC Facilitates Rad59-Dependent Homologous Recombination between Sister Chromatids by Promoting Cohesin Loading at DNA Double-Strand Breaks
- Creators
- Ji-Hyun Oum - Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245Changhyun Seong - Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520Youngho Kwon - Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520Jae-Hoon Ji - Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245Amy Sid - Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245Sreejith Ramakrishnan - Department of Biology, School of Science, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202-5132Grzegorz Ira - Department of Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030Anna Malkova - Department of Biology, School of Science, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202-5132Patrick Sung - Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520Sang Eun Lee - Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245Eun Yong Shim - Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245
- Resource Type
- Journal article
- Publication Details
- Molecular and cellular biology, Vol.31(19), pp.3924-3937
- DOI
- 10.1128/MCB.01269-10
- PMID
- 21807899
- PMCID
- PMC3187356
- NLM abbreviation
- Mol Cell Biol
- ISSN
- 0270-7306
- eISSN
- 1098-5549
- Publisher
- American Society for Microbiology
- Language
- English
- Date published
- 10/2011
- Academic Unit
- Biology
- Record Identifier
- 9984217540502771
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