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KMID : 0848120060310030081
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International Journal of Oral Biology
2006 Volume.31 No. 3 p.81 ~ p.86
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A Novel Histone Methyltransferase, Kodo7 Induces Histone H3-K9 Methylation and Mediates Apoptotic Cell Death
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Kim Sung-Mi
Seo Sang-Beom
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Abstract
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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.
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KEYWORD
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histone, methyltransferase, transcription, apoptosis
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