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

Molecular cell (2003-12-24)
Judd C Rice, Scott D Briggs, Beatrix Ueberheide, Cynthia M Barber, Jeffrey Shabanowitz, Donald F Hunt, Yoichi Shinkai, C David Allis
RESUMEN

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.

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Sigma-Aldrich
Anti-G9a Methyltransferase antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Histone H3 peptide (Di-methylated K9), biotin, ≥95% (HPLC)
Sigma-Aldrich
Histone H3 peptide (Tri-methylated K9), biotin, ≥90% (HPLC)
Sigma-Aldrich
Histone H3 peptide (Mono-methylated K9), biotin, ≥95% (HPLC)
Sigma-Aldrich
Anti-dimethyl-Histone H3 (diMe-Lys9) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

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