Chromatin Regulation / Acetylation

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Human histone methyltransferase SUV39H1 is the homolog of the dominant Drosophila PEV modifier Su(var)3-9 and is composed of 412 amino acid residues (1). It combines two of the most evolutionarily conserved domains of the "chromatin regulators": the chromo and SET domains (2,3). The 60 amino acid chromo domain represents an ancient histone-like fold that directs heterochromatic localizations. It has been demonstrated that the 130 amino acid SET domain contains the methyltransferase catalytic motif, which cooperates with the adjacent cysteine-rich regions to confer histone methyltransferase activity (1). This enzyme selectively methylates histone H3 on Lys9, which generates a binding site for HP1 proteins, a family of heterochromatic adaptor molecules involved in both gene silencing and supra-nucleosomal chromatin structure (4,5). SUV39H1 histone methyltransferase plays an important role in modification of histone amino termini and regulation of gene expression.

1. Rea, S. et al. (2000) Nature 406, 593-599.
2. Koonin, E. V. et al. (1995) Nucleic Acids Res. 23, 4229-4232.
3. Jenuwein, T. et al. (1998) Cell. Mol. Life Sci. 54, 80-93.
4. Lachner, M. et al. (2001) Nature 410, 116-120.
5. Bannister, A. J. et al. (2001) Nature 410, 120-123.

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SUV39H1 Histone Metyltransferase Antibody

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