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Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3.

We present evidence that both corepressors SMRT and N-CoR exist in large protein complexes with estimated sizes of 1.5-2 MDa in HeLa nuclear extracts. Using a combination of conventional and immunoaffinity chromatography, we have successfully isolated a SMRT complex and identified histone deacetylase 3 (HDAC3) and transducin (beta)-like I (TBL1), a WD-40 repeat-containing protein, as the subunits of the purified SMRT complex. We show that the HDAC3-containing SMRT and N-CoR complexes can bind to unliganded thyroid hormone receptors (TRs) in vitro. We demonstrate further that in Xenopus oocytes, both SMRT and N-CoR also associate with HDAC3 in large protein complexes and that injection of antibodies against HDAC3 or SMRT/N-CoR led to a partial relief of repression by unliganded TR/RXR. These findings thus establish both SMRT and N-CoR complexes as bona fide HDAC-containing complexes and shed new light on the molecular pathways by which N-CoR and SMRT function in transcriptional repression.

Pubmed ID: 10944117


  • Li J
  • Wang J
  • Wang J
  • Nawaz Z
  • Liu JM
  • Qin J
  • Wong J


The EMBO journal

Publication Data

August 15, 2000

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK 56324

Mesh Terms

  • Animals
  • Blotting, Western
  • Cell Nucleus
  • Chromatography, Affinity
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Cloning, Molecular
  • DNA-Binding Proteins
  • HeLa Cells
  • Histone Deacetylases
  • Humans
  • Ligands
  • Nuclear Proteins
  • Nuclear Receptor Co-Repressor 1
  • Nuclear Receptor Co-Repressor 2
  • Oocytes
  • Plasmids
  • Protein Binding
  • Receptors, Retinoic Acid
  • Receptors, Thyroid Hormone
  • Recombinant Proteins
  • Repressor Proteins
  • Transcription, Genetic
  • Two-Hybrid System Techniques
  • Xenopus