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

Abstract:

: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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Rice JC,Briggs SD,Ueberheide B,Barber CM,Shabanowitz J,Hunt DF,Shinkai Y,Allis CD

doi

10.1016/s1097-2765(03)00479-9

subject

Has Abstract

pub_date

2003-12-01 00:00:00

pages

1591-8

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(03)00479-9

journal_volume

12

pub_type

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