Structure and function of histone methylation binding proteins

被引：116

作者：

Adams-Cioaba, Melanie A. ^{[1
]}

Min, Jinrong ^{[1
,2
]}

机构：

[1] Univ Toronto, Struct Genom Consortium, Toronto, ON M5G 1L6, Canada

[2] Univ Toronto, Dept Physiol, Toronto, ON M5S 1A8, Canada

来源：

BIOCHEMISTRY AND CELL BIOLOGY | 2009年 / 87卷 / 01期

关键词：

chromatin remodeling; histone methylation; Tudor domain; MBT domain; PHD domain; PLANT HOMEODOMAIN FINGER; DE-NOVO METHYLATION; SMN TUDOR DOMAIN; PHD-FINGER; TUMOR-SUPPRESSOR; GENE-EXPRESSION; DROSOPHILA-MELANOGASTER; LYSINE METHYLATION; MOLECULAR-BASIS; POLYCOMB GROUP;

D O I：

10.1139/O08-129

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Chromatin structure is regulated by chromatin remodeling factors, histone exchange, linker histone association, and histone modification. Covalent modification of histones is an important factor in the regulation of the associated processes. The implementation and removal of various histone modifications have been implicated in DNA replication, repair, recombination, and transcription, and in RNA processing. In recent years, histone methylation has emerged as one of the key modifications regulating chromatin function. However, the mechanisms involved are complex and not well understood. A large volume of structural and biochemical information has been recently amassed for the Tudor, plant homeodomain (PHD), and malignant brain tumor (MBT) protein families. This review summarizes current knowledge of the structures and modes of recognition employed by the PHD, Tudor, and MBT domains in their interactions with target histone peptides.

引用

页码：93 / 105

页数：13

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