Journal article
The emerging roles of ATP-dependent chromatin remodeling enzymes in nucleotide excision repair
International journal of molecular sciences, Vol.13(9), pp.11954-11973
2012
Handle:
https://hdl.handle.net/2376/102217
PMCID: PMC3472786
PMID: 23109894
Abstract
DNA repair in eukaryotic cells takes place in the context of chromatin, where DNA, including damaged DNA, is tightly packed into nucleosomes and higher order chromatin structures. Chromatin intrinsically restricts accessibility of DNA repair proteins to the damaged DNA and impacts upon the overall rate of DNA repair. Chromatin is highly responsive to DNA damage and undergoes specific remodeling to facilitate DNA repair. How damaged DNA is accessed, repaired and restored to the original chromatin state, and how chromatin remodeling coordinates these processes in vivo, remains largely unknown. ATP-dependent chromatin remodelers (ACRs) are the master regulators of chromatin structure and dynamics. Conserved from yeast to humans, ACRs utilize the energy of ATP to reorganize packing of chromatin and control DNA accessibility by sliding, ejecting or restructuring nucleosomes. Several studies have demonstrated that ATP-dependent remodeling activity of ACRs plays important roles in coordination of spatio-temporal steps of different DNA repair pathways in chromatin. This review focuses on the role of ACRs in regulation of various aspects of nucleotide excision repair (NER) in the context of chromatin. We discuss current understanding of ATP-dependent chromatin remodeling by various subfamilies of remodelers and regulation of the NER pathway in vivo.
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Details
- Title
- The emerging roles of ATP-dependent chromatin remodeling enzymes in nucleotide excision repair
- Creators
- Wioletta Czaja - Biochemistry and Biophysics, School of Molecular Biosciences, Washington State University, Pullman, WA, USA; E-Mails: wiolettapyrzak@vetmed.wsu.edu (W.C.); pengmao@vetmed.wsu.edu (P.M.)Peng MaoMichael J Smerdon
- Publication Details
- International journal of molecular sciences, Vol.13(9), pp.11954-11973
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- Switzerland
- Grant note
- R01 ES004106 / NIEHS NIH HHS R37 ES002614 / NIEHS NIH HHS ES004106 / NIEHS NIH HHS R01 ES002614 / NIEHS NIH HHS ES002614 / NIEHS NIH HHS
- Identifiers
- 99900546544701842
- Language
- English
- Resource Type
- Journal article