Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly

被引：1388

作者：

Nakayam, J

Rice, JC

Strahl, BD

Allis, CD

Grewal, SIS

机构：

[1] Cold Spring Harbor Lab, Cold Spring Harbor, NY 11724 USA

[2] Univ Virginia, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA

来源：

SCIENCE | 2001年 / 292卷 / 5514期

关键词：

D O I：

10.1126/science.1060118

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The assembly of higher order chromatin structures has been Linked to the covalent modifications of histone tails. We provide in vivo evidence that lysine 9 of histone H3 (H3 Lys(9)) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast. Both the conserved chromo- and SET domains of Clr4 are required for H3 Lys(9) methylation in vivo. Localization of Swi6, a homolog of Drosophila HP1, to heterochomatic regions is dependent on H3 Lysg methylation. Moreover, an H3-specific deacetylase Clr3 and a beta -propeller domain protein Rik1 are required for H3 Lys(9) methylation by Clr4 and Swi6 Localization. These data define a conserved pathway wherein sequential histone modifications establish a "histone code" essential for the epigenetic inheritance of heterochromatin assembly.

引用

页码：110 / 113

页数：4

共 30 条

[1] Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 [J].