The SANT domain: a unique histone-tail-binding module?

被引：309

作者：

Boyer, LA

Latek, RR

Peterson, CL

机构：

[1] Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01065 USA

[2] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2004年 / 5卷 / 02期

关键词：

D O I：

10.1038/nrm1314

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Chromatin-remodelling complexes have an important role in all DNA-mediated processes and, although much is known about how these enzymes regulate chromosomal DNA accessibility, how they interact with their histone substrates has remained unclear. However, recent studies have indicated that the SANT domain has a central role in chromatin remodelling by functioning as a unique histone-interaction module that couples histone binding to enzyme catalysis.

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页码：158 / 163

页数：6

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