Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains

被引：632

作者：

Rice, JC

Briggs, SD

Ueberheide, B

Barber, CM

Shabanowitz, J

Hunt, DF

Shinkai, Y

Allis, CD

机构：

[1] Univ Virginia, Dept Biochem & Mol Genet, Hlth Syst, Charlottesville, VA 22908 USA

[2] Univ Virginia, Dept Chem, Charlottesville, VA 22908 USA

[3] Univ Virginia, Dept Pathol, Charlottesville, VA 22904 USA

[4] Kyoto Univ, Inst Virus Res, Dept Cell Biol, Kyoto 6068507, Japan

来源：

MOLECULAR CELL | 2003年 / 12卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(03)00479-9

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：

The functional significance of mono-, di-, and trimethylation of lysine residues within histone proteins remains unclear. Antibodies developed to selectively recognize each of these methylated states at histone H3 lysine 9 (H3 Lys9) demonstrated that mono- and dimethylation localized specifically to silent domains within euchromatin. In contrast, trimethylated H3 Lys9 was enriched at pericentric heterochromatin. Enzymes known to methylate H3 Lys9 displayed remarkably different enzymatic properties in vivo. G9a was responsible for all detectable H3 Lys9 dimethylation and a significant amount of monomethylation within silent euchromatin. In contrast, Suv39h1 and Suv39h2 directed H3 Lys9 trimethylation specifically at pericentric heterochromatin. Thus, different methylated states of H3 Lys9 are directed by specific histone methyltransferases to "mark" distinct domains of silent chromatin.

引用

页码：1591 / 1598

页数：8

共 27 条

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