NuA4 acetyltransferase is required for efficient nucleotide excision repair in yeast.
NuA4 acetyltransferase is required for efficient nucleotide excision repair in yeast.
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DOI：
10.1016/j.dnarep.2018.11.006
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发表时间：
2019-01
期刊：
影响因子：
3.8
通讯作者：
Wyrick JJ
中科院分区：
文献类型：
--
作者：
Hodges AJ;Plummer DA;Wyrick JJ
核苷酸切除修复（NER）途径对于从细胞DNA去除由紫外线（UV）光和其他螺旋扭曲损伤诱导的损伤至关重要。虽然有效的NER对于避免细胞死亡和诱变是至关重要的，但由于含有损伤的DNA与组蛋白的结合，NER活性在染色质中被抑制。组蛋白乙酰化已成为促进染色质中NER的重要机制，特别是Spt-Ada-Gcn 5乙酰转移酶（佐贺）催化的乙酰化;然而，尚不清楚其他组蛋白乙酰转移酶（HAT）是否促进染色质中的NER活性。在这里，我们报告说，必要的核小体乙酰转移酶组蛋白H4（NuA 4）复合物是必需的有效NER在酿酒酵母。NuA 4复合物的非必需Yng 2亚基的缺失导致酵母中UV诱导的环丁烷嘧啶二聚体（CPD）修复的一般缺陷;相反，NuA 3复合物的Sas 3催化亚基的缺失不影响修复。快速耗尽的基本NuA 4催化亚基Esa 1使用锚的方法也会导致NER的缺陷，特别是在异染色质HML基因座。我们发现，破坏Rpd 3L组蛋白脱乙酰酶（HDAC）复合物的Sds 3亚基拯救了与Esa 1活性丧失相关的修复缺陷，这表明NuA 4催化的乙酰化对于异染色质中的高效NER是重要的。
The nucleotide excision repair (NER) pathway is critical for removing damage induced by ultraviolet (UV) light and other helix-distorting lesions from cellular DNA. While efficient NER is critical to avoid cell death and mutagenesis, NER activity is inhibited in chromatin due to the association of lesion-containing DNA with histone proteins. Histone acetylation has emerged as an important mechanism for facilitating NER in chromatin, particularly acetylation catalyzed by the Spt-Ada-Gcn5 acetyltransferase (SAGA); however, it is not known if other histone acetyltransferases (HATs) promote NER activity in chromatin. Here, we report that the essential Nucleosome Acetyltransferase of histone H4 (NuA4) complex is required for efficient NER in Saccharomyces cerevisiae. Deletion of the non-essential Yng2 subunit of the NuA4 complex causes a general defect in repair of UV-induced cyclobutane pyrimidine dimers (CPDs) in yeast; in contrast, deletion of the Sas3 catalytic subunit of the NuA3 complex does not affect repair. Rapid depletion of the essential NuA4 catalytic subunit Esa1 using the anchor-away method also causes a defect in NER, particularly at the heterochromatic HML locus. We show that disrupting the Sds3 subunit of the Rpd3L histone deacetylase (HDAC) complex rescued the repair defect associated with loss of Esa1 activity, suggesting that NuA4-catalyzed acetylation is important for efficient NER in heterochromatin.
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