| First Author | Kim SM | Year | 2007 |
| Journal | Exp Cell Res | Volume | 313 |
| Issue | 5 | Pages | 975-83 |
| PubMed ID | 17239852 | Mgi Jnum | J:119511 |
| Mgi Id | MGI:3702361 | Doi | 10.1016/j.yexcr.2006.12.007 |
| Citation | Kim SM, et al. (2007) The histone methyltransferase activity of WHISTLE is important for the induction of apoptosis and HDAC1-mediated transcriptional repression. Exp Cell Res 313(5):975-83 |
| abstractText | Posttranslational histone methylation has been correlated with transcriptional regulation. However, the functional significance of methylation of lysine residues of histone remains largely unknown. Previously, we have characterized a novel histone methyltransferase (HMTase), WHISTLE which methylates histone H3-K4 and H3-K27 to repress transcription. In this study, we demonstrated that WHISTLE can induce apoptotic cell death through caspase-3 activation and that HMTase activity is important for the apoptosis induction. Deletion mapping analysis elicited that N-terminus PWWP region is required for HMTase activity by interacting with putative associating factors. Point mutant analysis revealed that SET domain cysteine 297 is a critical residue for the HMTase activity of WHISTLE. WHISTLE repressed transcription through HDAC1 recruitment possibly through the N-terminus region. Our results suggest that HMTase WHISTLE induces apoptosis in an HMTase activity-dependent manner and represses transcription of target genes through HDAC1 recruitment. |
