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A Novel Histone Methyltransferase, Kodo7 Induces Histone H3-K9 Methylation and Mediates Apoptotic Cell Death  

Kim, Sung-Mi (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Seo, Sang-Beom (Department of Life Science, College of Natural Sciences, Chung-Ang University)
Publication Information
International Journal of Oral Biology / v.31, no.3, 2006 , pp. 81-86 More about this Journal
Abstract
SET (Suppressor of variegation, Enhancer of zeste, and the Trithorax) domain-containing proteins are known to have methyltransferase activity at lysine residues of histone proteins. In this study, we identified a novel SET domain-containing protein from mouse and named Kodo7. Indeed, Kodo7 has methyltransferase activity at K9 residue of the H3 protein as demonstrated by a histone methyl-transferse activity assay using GST-tagged Kodo7. Confocal microscopy showed that Kodo7 is co-localized with histones in the nucleus. Interestingly, ectopic expression of Kodo7 by transient transfection induced cell death and treatment of the transfectants with a caspase-3 inhibitor, Ac-DEVD-AFC decreased Kodo7-induced apoptosis. These results suggest that Kodo7 induces apoptotic cell death through increased methylation of histones leading to transcriptional repression.
Keywords
histone; methyltransferase; transcription; apoptosis;
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