Structure and function of bromodomains in chromatin-regulating complexes

被引：70

作者：

Marmorstein, R

Berger, SL

机构：

[1] Wistar Inst Anat & Biol, Mol Genet Program, Philadelphia, PA 19104 USA

[2] Wistar Inst Anat & Biol, Struct Biol Program, Philadelphia, PA 19104 USA

来源：

GENE | 2001年 / 272卷 / 1-2期

关键词：

histone; nucleosome; acetylation; transcriptional regulation;

D O I：

10.1016/S0378-1119(01)00519-4

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Specific changes in chromatin structure are associated with transcriptional regulation. These chromatin alterations include both covalent modifications of the amino termini of histones as well as ATP-dependent non-covalent remodeling of nucleosomes. Certain protein domains, such as the bromodomains, are commonly associated with both of these classes of enzymes that alter chromatin. This review discusses recent advances in understanding the structure and function of bromodomains. Most significantly, a role of bromodomains has been revealed in binding to acetylated lysine residues in histone tails. Interactions between bromodomains and modified histones may be an important mechanism underlying chromatin structural changes and gene regulation. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：1 / 9

页数：9

共 45 条

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