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Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.

The human thyroid hormone receptor-associated protein (TRAP) complex, an earlier described coactivator for nuclear receptors, and an SRB- and MED-containing cofactor complex (SMCC) that mediates activation by Gal4-p53 are shown to be virtually the same with respect to specific polypeptide subunits, coactivator functions, and mechanisms of action (activator interactions). In parallel with ligand-dependent interactions of nuclear receptors with the TRAP220 subunit, p53 and VP16 activation domains interact directly with a newly cloned TRAP80 subunit. These results indicate novel pathways for the function of nuclear receptors and other activators (p53 and VP16) through a common coactivator complex that is likely to target RNA polymerase II. Identification of the TRAP230 subunit as a previously predicted gene product also suggests a coactivator-related transcription defect in certain disease states.

Pubmed ID: 10198638


  • Ito M
  • Yuan CX
  • Malik S
  • Gu W
  • Fondell JD
  • Yamamura S
  • Fu ZY
  • Zhang X
  • Qin J
  • Roeder RG


Molecular cell

Publication Data

March 26, 1999

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Blotting, Northern
  • Blotting, Western
  • Carrier Proteins
  • Cloning, Molecular
  • Fungal Proteins
  • Gene Expression Regulation
  • HeLa Cells
  • Herpes Simplex Virus Protein Vmw65
  • Humans
  • Mediator Complex
  • Mediator Complex Subunit 1
  • Molecular Sequence Data
  • Protein Binding
  • RNA Polymerase II
  • Receptors, Calcitriol
  • Receptors, Thyroid Hormone
  • Response Elements
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors
  • Tumor Suppressor Protein p53