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Nat Struct Mol Biol. 2011 Feb;18(2):177-84. doi: 10.1038/nsmb.1983. Epub 2011 Jan 16.

Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery.

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  • 1Henry Wellcome Laboratories of Structural Biology, Department of Biochemistry, University of Leicester, Leicester, UK.

Abstract

Eukaryotic transcriptional repressors function by recruiting large coregulatory complexes that target histone deacetylase enzymes to gene promoters and enhancers. Transcriptional repression complexes, assembled by the corepressor NCoR and its homolog SMRT, are crucial in many processes, including development and metabolic physiology. The core repression complex involves the recruitment of three proteins, HDAC3, GPS2 and TBL1, to a highly conserved repression domain within SMRT and NCoR. We have used structural and functional approaches to gain insight into the architecture and biological role of this complex. We report the crystal structure of the tetrameric oligomerization domain of TBL1, which interacts with both SMRT and GPS2, and the NMR structure of the interface complex between GPS2 and SMRT. These structures, together with computational docking, mutagenesis and functional assays, reveal the assembly mechanism and stoichiometry of the corepressor complex.

PMID:
21240272
[PubMed - indexed for MEDLINE]
PMCID:
PMC3232451
Free PMC Article
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