组蛋白乙酰转移酶复合物：并非一概而论。

Histone acetyltransferase complexes: one size doesn't fit all.

作者信息

Lee Kenneth K, Workman Jerry L

机构信息

Stowers Institute, 1000 East 50th Street, Kansas City, Missouri 64110, USA.

出版信息

Nat Rev Mol Cell Biol. 2007 Apr;8(4):284-95. doi: 10.1038/nrm2145.

DOI:10.1038/nrm2145

PMID:17380162

Abstract

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.

摘要

在过去十年中，组蛋白乙酰转移酶（HATs）的研究取得了显著进展，并且已经从各种生物体中分离出了多种HATs。结果表明，HATs具有高度多样性，通常包含多个亚基。催化亚基的功能在很大程度上取决于复合物中其他亚基的背景。我们才刚刚开始了解HAT复合物在染色体解聚、DNA损伤修复和非组蛋白底物修饰中的特殊作用，以及它们在更广泛的表观遗传格局中的作用，包括HAT复合物内蛋白质结构域的作用以及HAT复合物与现有组蛋白修饰之间的动态相互作用。