Journal article
Histone H3 Lysine 14 (H3K14) Acetylation Facilitates DNA Repair in a Positioned Nucleosome by Stabilizing the Binding of the Chromatin Remodeler RSC (Remodels Structure of Chromatin)
The Journal of biological chemistry, Vol.289(12), pp.8353-8363
03/21/2014
Handle:
https://hdl.handle.net/2376/104364
PMCID: PMC3961661
PMID: 24515106
Abstract
Background:
Histone H3K14 acetylation is induced by UV damage.
Results:
Nucleosomes with acetylated H3K14 show greater CPD repair than unacetylated nucleosomes in the presence of the chromatin remodeling complex RSC.
Conclusion:
H3K14ac acts as a “docking site” to retain RSC on nucleosomes and facilitate DNA repair.
Significance:
DNA repair is accelerated by an orchestrated action between UV-induced histone acetylation and chromatin remodeling.
Histone H3 acetylation is induced by UV damage in yeast and may play an important role in regulating the repair of UV photolesions in nucleosome-loaded genomic loci. However, it remains elusive how H3 acetylation facilitates repair. We generated a strongly positioned nucleosome containing homogeneously acetylated H3 at Lys-14 (H3K14ac) and investigated possible mechanisms by which H3K14 acetylation modulates repair. We show that H3K14ac does not alter nucleosome unfolding dynamics or enhance the repair of UV-induced cyclobutane pyrimidine dimers by UV photolyase. Importantly, however, nucleosomes with H3K14ac have a higher affinity for purified chromatin remodeling complex RSC (Remodels the Structure of Chromatin) and show greater cyclobutane pyrimidine dimer repair compared with unacetylated nucleosomes. Our study indicates that, by anchoring RSC, H3K14 acetylation plays an important role in the unfolding of strongly positioned nucleosomes during repair of UV damage.
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Details
- Title
- Histone H3 Lysine 14 (H3K14) Acetylation Facilitates DNA Repair in a Positioned Nucleosome by Stabilizing the Binding of the Chromatin Remodeler RSC (Remodels Structure of Chromatin)
- Creators
- Ming-Rui Duan - From Biochemistry and Biophysics, School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-7520Michael J Smerdon - From Biochemistry and Biophysics, School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-7520
- Publication Details
- The Journal of biological chemistry, Vol.289(12), pp.8353-8363
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- American Society for Biochemistry and Molecular Biology; 9650 Rockville Pike, Bethesda, MD 20814, U.S.A
- Grant note
- ES004106 / National Institutes of Health
- Identifiers
- 99900547090801842
- Language
- English
- Resource Type
- Journal article