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J Biol Chem, Vol. 274, Issue 47, 33194-33197, November 19, 1999
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From the Transcriptional repression by sequence-specific DNA
binding factors is mediated by the recruitment of a corepressor complex to the promoter region. The NK-3 homeodomain protein is a
transcriptional repressor that recruits the nuclear protein kinase,
homeodomain interacting protein kinase 2 (HIPK2). Here we show that
HIPK2 is a component of a corepressor complex containing Groucho and a
histone deacetylase complex. Groucho, like HIPK2, acts as a corepressor
for NK-3 and binds to NK-3 and HIPK2. Moreover, HIPK2 appears to
regulate the corepressor activity of Groucho. Transcriptional repression by NK-3 and Groucho is relieved by the histone deacetylase inhibitor trichostatin A, and both NK-3 and Groucho directly interact with the histone deacetylase HDAC1 that is associated with mSin3A in vivo. Recruitment of the histone deacetylase complex by
NK-3 decreases the acetylated histones that are associated with the target gene promoter. These results indicate that NK-3 represses transcription by recruiting a complex containing Groucho and a histone
deacetylase complex that leads to histone modification on chromatin and
suggest that HIPK2 may play a regulatory role in the corepressor
complex formation.
Laboratory of Molecular Cardiology, NHLBI,
National Institutes of Health, Bethesda, Maryland 20892 and the
§ Department of Radiation Medicine, Georgetown University,
Washington, D. C. 20007
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