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

Jasmeen Oberoi, Louise Fairall, Peter J. Watson, Ji Chun Yang, Zsolt Czimmerer, Thorsten Kampmann, Benjamin T. Goult, Jacquie A. Greenwood, John T. Gooch, Bettina C. Kallenberger, Laszlo Nagy, David Neuhaus, John W.R. Schwabe

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)177-185
Number of pages9
JournalNature Structural and Molecular Biology
Issue number2
StatePublished - Feb 2011
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


Dive into the research topics of 'Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery'. Together they form a unique fingerprint.

Cite this