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XB-ART-49792
Biochem J 2014 Jul 15;4612:323-34. doi: 10.1042/BJ20140374.
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Characterization of the histone methyltransferase PRDM9 using biochemical, biophysical and chemical biology techniques.

Koh-Stenta X , Joy J , Poulsen A , Li R , Tan Y , Shim Y , Min JH , Wu L , Ngo A , Peng J , Seetoh WG , Cao J , Wee JL , Kwek PZ , Hung A , Lakshmanan U , Flotow H , Guccione E , Hill J .


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PRDM proteins have emerged as important regulators of disease and developmental processes. To gain insight into the mechanistic actions of the PRDM family, we have performed comprehensive characterization of a prototype member protein, the histone methyltransferase PRDM9, using biochemical, biophysical and chemical biology techniques. In the present paper we report the first known molecular characterization of a PRDM9-methylated recombinant histone octamer and the identification of new histone substrates for the enzyme. A single C321P mutant of the PR/SET domain was demonstrated to significantly weaken PRDM9 activity. Additionally, we have optimized a robust biochemical assay amenable to high-throughput screening to facilitate the generation of small-molecule chemical probes for this protein family. The present study has provided valuable insight into the enzymology of an intrinsically active PRDM protein.

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Species referenced: Xenopus laevis
Genes referenced: XB5904899