SUV39H1 is a human histone methyltransferase that modifies lysine 9 in the amino-terminal region of histone H3. Its catalytic machinery includes a SET domain and adjoining cysteine-rich regions. The corresponding gene encodes an enzyme acting on a protein component of chromatin.[ref]
Regulation of chromatin structure by site-specific histone H3 methyltransferases by S. Rea and others. 2000, abstract: human SUV39H1, H3 lysine 9 specificity and required regions
The original biochemical work established site specificity using histone H3 substrates and mapped the catalytic requirement to regions of SUV39H1. It also found that lysine 9 methylation interfered with phosphorylation of neighbouring serine 10. This gives an illuminating example of interacting histone modifications: changing one residue can affect a modification at the next residue, so the histone tail is a chemically coupled substrate.[ref]
Regulation of chromatin structure by site-specific histone H3 methyltransferases by S. Rea and others. Abstract: substrate specificity, domain mapping and interaction with serine 10 phosphorylation
For an enzyme assay, the informative measurement is formation of the specified methylated histone product. Simply detecting SUV39H1 expression establishes the presence of its protein, while activity additionally depends on the reaction conditions and available substrate.
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