Histone methyltransferases catalyze the transfer of methyl groups to histone proteins, affecting gene expression. Aberrant methylation has been demonstrated in various disease states; therefore, knowledge of the structure and kinetics of the enzymes can aid in understanding the disease mechanism. PRDM2 is a histone lysine methyltransferase important in cell division and differentiation that has been linked to human cancers. Work on a similar enzyme showed that a conformational change in the enzyme is needed to create the active site and enable methyltransferase activity. While NMR and X-ray crystal structures of PRDM2 have been solved, all structures involved inactive truncations of the enzyme missing the amino acids likely to be involved in the conformational change. This work aims to use IR spectroscopy to assess structural changes in kinetically active wild type and mutant variants of the catalytic domain to shed light on the general mechanism of action of PRDM2 and its role in human cancers.

Investigation of conformational changes in histone methyltransferase PRDM2 catalytic domain variants

2019 Fall National Meeting

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