SUV39H1 (D11B6) Rabbit mAb #8729

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.