Cited by 165Genomics and Chromatin DynamicsProtein Structure and DynamicsHistone Deacetylase Inhibitors Research

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

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Oberoi, Jasmeen, Fairall, Louise, Watson, Peter J, Yang, Ji-Chun, Czimmerer, Zsolt, Kampmann, Thorsten, Goult, Benjamin T, Greenwood, Jacquie A +5 more·2011·Nature Structural & Molecular Biology

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.

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  • HDAC3 appears to be uniquely recruited to the SMRT/NCoR complex, where it interacts with a conserved deacetylase-activation-domain (DAD) within SMRT or NCoR.

    “In contrast, HDAC3 appears to be uniquely recruited to the SMRT/NCoR complex where it interacts with a conserved deacetylase-activation-domain (DAD) within SMRT or NCoR8,10,12,24,25,26.”

    From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [26]

    The introductory passage labelled Abstract (page unavailable) says HDAC3 is recruited to the SMRT/NCoR complex and interacts with the SMRT deacetylase activation domain. It also says the complexes associate with multiple histone deacetylases, so it does not establish that HDAC3 is uniquely recruited. The passage does not explicitly describe an interaction with the NCoR DAD. (LLM, conf=0.85)

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Research works printed but not linked: 3

  1. [11]Barroso I Dominant negative mutations in human PPARgamma associated with severe insulin resistance Nature 1999 402 880 883 10622252
  2. [36]Choi HK Function of Multiple LisH/WD-40 Repeat-Containing Proteins in Feed-Forward Transcriptional Repression by SMRT/N-CoR Corepressor Complexes Mol Endocrinol 2008 18202150 PMC5419524
  3. [57]McCoy AJ Phaser crystallographic software J Appl Crystallogr 2007 40 658 674 19461840 PMC2483472

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Authors
Oberoi, J., Fairall, L., Watson, P. J., Yang, J.-C., Czimmerer, Z., Kampmann, T., Goult, B. T., Greenwood, J. A., Gooch, J. T., Kallenberger, B. C., Nagy, L., Neuhaus, D., & Schwabe, J. W. R.
Affiliations
  • University of Leicester (GB)
  • MRC Laboratory of Molecular Biology (GB)
  • University of Debrecen (HU)
Corresponding author
Schwabe, John W R
Venue
Nature Structural & Molecular Biology
Published
2011-01-16
Volume
18
Issue
2
Pages
177-184
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2064488190
Cited by
165
References
61
Citations by year
2026: 8 · 2025: 8 · 2024: 11 · 2023: 10 · 2022: 8 · 2021: 10 · 2020: 21 · 2019: 12 · 2018: 7 · 2017: 11 · 2016: 10 · 2015: 11 · 2014: 8 · 2013: 13 · 2012: 13
FWCI
4.93
Type
journal article
Language
en
Open access
Locations
  • Nature Structural & Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
  • Kent Academic Repository (University of Kent) (submittedVersion)
  • Leicester Research Archive (University of Leicester) (submittedVersion)
Funders
  • Wellcome Trust (085408)
  • European Synchrotron Radiation Facility
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Keywords
SMRT, NCoR, corepressor complex, transcriptional repression, TBL1, GPS2, HDAC3, histone deacetylase, protein complex formation, oligomerization domain, crystal structure, NMR structure, protein-protein interaction, stoichiometry
MeSH terms
Amino Acid Sequence, Animals, Cell Line, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Transducin, Protein Structure, Tertiary, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Amino Acid Motifs, Intracellular Signaling Peptides and Proteins, Mice, Protein Multimerization, Nuclear Receptor Co-Repressor 2

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