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Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha.

Transcriptional coactivators showing physical and functional interactions with PPARgamma include the protein acetyl transferase p300, the TRAP/Mediator complex that interacts with the general transcription machinery, and the highly regulated PGC-1alpha. We show that PGC-1alpha directly interacts with TRAP/Mediator, through the PPARgamma-interacting subunit TRAP220, and stimulates TRAP/Mediator-dependent function on DNA templates. Further, while ineffective by itself, PGC-1alpha stimulates p300-dependent histone acetylation and transcription on chromatin templates in response to PPARgamma. These functions are mediated by largely independent PPARgamma, p300, and TRAP220 interaction domains in PGC-1alpha, whereas p300 and TRAP220 show ligand-dependent interactions with a common region of PPARgamma. Apart from showing PGC-1alpha functions both in chromatin remodeling and in preinitiation complex formation or function (transcription), these results suggest a key role for PGC-1alpha, through concerted but dynamic interactions, in coordinating these steps.

Pubmed ID: 14636573


  • Wallberg AE
  • Yamamura S
  • Malik S
  • Spiegelman BM
  • Roeder RG


Molecular cell

Publication Data

November 25, 2003

Associated Grants

  • Agency: NCI NIH HHS, Id: CA42567

Mesh Terms

  • Animals
  • Chromatin
  • E1A-Associated p300 Protein
  • Genes, Reporter
  • HeLa Cells
  • Humans
  • Mediator Complex
  • Mediator Complex Subunit 1
  • Mice
  • Nuclear Proteins
  • Protein Subunits
  • Receptors, Cytoplasmic and Nuclear
  • Recombinant Fusion Proteins
  • Trans-Activators
  • Transcription Factors
  • Transcription, Genetic