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 Celljournal_title
Molecular cellauthors
Rice JC,Briggs SD,Ueberheide B,Barber CM,Shabanowitz J,Hunt DF,Shinkai Y,Allis CDdoi
10.1016/s1097-2765(03)00479-9subject
Has Abstractpub_date
2003-12-01 00:00:00pages
1591-8issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(03)00479-9journal_volume
12pub_type
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