首页> 美国卫生研究院文献>The Journal of Biological Chemistry >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)
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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)

机译:组蛋白H3赖氨酸14(H3K14)乙酰化通过稳定染色质重塑剂RSC的结合(重塑染色质结构)促进定位核小体中的DNA修复

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摘要

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.
机译:组蛋白H3乙酰化是由酵母中的UV损伤诱导的,并且可能在调节装载有核小体的基因组基因座中对UV光损伤的修复中起重要作用。然而,仍然不清楚H 3乙酰化如何促进修复。我们产生了一个强定位的核小体,在Lys-14(H3K14ac)处含有均一的乙酰化H3,并研究了H3K14乙酰化调节修复的可能机制。我们表明,H3K14ac不会改变核小体展开动力学,也不会通过紫外线光解酶增强紫外线诱导的环丁烷嘧啶二聚体的修复。然而,重要的是,与未乙酰化的核小体相比,具有H3K14ac的核小体对纯化的染色质重塑复合体RSC(重塑染色质的结构)具有更高的亲和力,并显示出更大的环丁烷嘧啶二聚体修复。我们的研究表明,通过锚定RSC,H3K14乙酰化在修复紫外线损伤过程中在强定位核小体的展开中起重要作用。

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