The homeodomain protein NK-3 recruits Groucho and a histone deacetylase complex to repress transcription

Cheol Yong Choi, Young Ho Kim, Ho Jeong Kwon, Yongsok Kim

Research output: Contribution to journalArticle

134 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)33194-33197
Number of pages4
JournalJournal of Biological Chemistry
Volume274
Issue number47
DOIs
Publication statusPublished - 1999 Nov 19

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Homeodomain Proteins
Histone Deacetylases
Transcription
Protein Kinases
Co-Repressor Proteins
Histones
trichostatin A
Histone Code
Histone Deacetylase 1
Histone Deacetylase Inhibitors
Nuclear Proteins
Genetic Promoter Regions
Chromatin
Genes
DNA

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "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.",
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The homeodomain protein NK-3 recruits Groucho and a histone deacetylase complex to repress transcription. / Choi, Cheol Yong; Kim, Young Ho; Kwon, Ho Jeong; Kim, Yongsok.

In: Journal of Biological Chemistry, Vol. 274, No. 47, 19.11.1999, p. 33194-33197.

Research output: Contribution to journalArticle

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