| First Author | Koh-Stenta X | Year | 2014 |
| Journal | Biochem J | Volume | 461 |
| Issue | 2 | Pages | 323-34 |
| PubMed ID | 24785241 | Mgi Jnum | J:215270 |
| Mgi Id | MGI:5604977 | Doi | 10.1042/BJ20140374 |
| Citation | Koh-Stenta X, et al. (2014) Characterization of the histone methyltransferase PRDM9 using biochemical, biophysical and chemical biology techniques. Biochem J 461(2):323-34 |
| abstractText | 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. |
