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The histone methyltransferase activity of WHISTLE is important for the induction of apoptosis and HDAC1-mediated transcriptional repression
- Source :
-
Experimental Cell Research . Mar2007, Vol. 313 Issue 5, p975-983. 9p. - Publication Year :
- 2007
-
Abstract
- Abstract: 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. [Copyright &y& Elsevier]
- Subjects :
- *HISTONES
*METHYLTRANSFERASES
*APOPTOSIS
*METHYLATION
Subjects
Details
- Language :
- English
- ISSN :
- 00144827
- Volume :
- 313
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Experimental Cell Research
- Publication Type :
- Academic Journal
- Accession number :
- 24148733
- Full Text :
- https://doi.org/10.1016/j.yexcr.2006.12.007