Andrei Kuzmichev 2026-11-05
Andrei Kuzmichev led a 2002 study identifying histone methyltransferase activity in a human protein complex containing Enhancer of Zeste. Biochemical isolation linked the complex to methylation of histone H3, with activity depending on an intact SET domain.[ref]
Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein by Andrei Kuzmichev and others. Abstract: isolated complex, histone substrates and SET-domain requirement
The contribution connected a regulator of gene expression to a specific chemical activity on chromatin. Measuring a histone methylation reaction and disrupting a required domain supplied more mechanistic information than observing that two proteins occur in the same cell.
H3K27 methylation 2026-11-05
H3K27 methylation is addition of one or more methyl groups to the side chain of lysine 27 in histone H3. Mono-, di- and trimethylated states are different chemical states; a measurement of one is not automatically a measurement of the others. H3K27 trimethylation is particularly associated with Polycomb-mediated gene silencing. [ref]
A mechanistic test distinguishes correlation from catalysis. A purified complex can be supplied with histones and a methyl donor to test transfer, while changing a catalytic region tests whether that activity depends on an intact enzyme. In a cell, the distribution of the mark also depends on recruitment, removal and replacement of histones, not only on total enzyme abundance.