Published online 18 November 2004
Nucleic Acids Research, Vol. 32 No. 20 © Oxford University Press 2004; all rights reserved
Functional role of G9a-induced histone methylation in small heterodimer partner-mediated transcriptional repression
Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas, PO Box 1527, Vassilika Vouton, 711 10 Herakleion, Crete, Greece
* To whom correspondence should be addressed: Tel: +30 2810 391163; Fax: +30 2810 391101; Email: talianid{at}imbb.forth.gr
Received September 2, 2004; Revised October 20, 2004; Accepted October 29, 2004
Site-specific modification of nucleosomal histones plays a central role in the formation of transcriptionally active and inactive chromatin structures. These modifications may serve as specific recognition motifs for chromatin proteins, which act as a signal for the adoption of the appropriate regulatory responses. Here, we show that the orphan nuclear receptor SHP (small heterodimer partner), a coregulator that inhibits the activity of several nuclear receptors, can associate with unmodified and lysine 9-methylated histone-3, but not with the acetylated protein. The naturally occurring SHP mutant (R213C), which exhibits decreased transrepression potential, interacts less avidly with K9-methylated histone 3. We demonstrate that SHP can functionally interact with histone deacetylase-1 and the G9a methyltransferase and that it is localized exclusively in nuclease-sensitive euchromatin. The results point to the involvement of a multistep mechanism in SHP-dependent transcriptional repression, which includes histone deacetylation, followed by H3-K9 methylation and stable association of SHP itself with chromatin.
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