Histone acetyltransferase complexes: one size doesn't fit all

被引：798

作者：

Lee, Kenneth K. ^{[1
]}

Workman, Jerry L. ^{[1
]}

机构：

[1] Stowers Inc, Kansas City, MO 64110 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2007年 / 8卷 / 04期

基金：

美国国家卫生研究院;

关键词：

NUCLEOTIDE EXCISION-REPAIR; DNA-DEPENDENT ACETYLATION; DROSOPHILA MSL COMPLEX; DOSAGE COMPENSATION; CHROMATIN-STRUCTURE; PROTEIN COMPLEX; SACCHAROMYCES-CEREVISIAE; SILENCING PROTEIN; DIVERSE FUNCTIONS; CRYSTAL-STRUCTURE;

D O I：

10.1038/nrm2145

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on the context of the other subunits in the complex. We are just beginning to understand the specialized roles of HAT complexes in chromosome decondensation, DNA-damage repair and the modification of non-histone substrates, as well as their role in the broader epigenetic landscape, including the role of protein domains within HAT complexes and the dynamic interplay between HAT complexes and existing histone modifications.

引用

页码：284 / 295

页数：12

共 132 条

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