Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations

J Biol Chem. 1998 Oct 30;273(44):28564-7. doi: 10.1074/jbc.273.44.28564.

Abstract

Steroid receptor coactivator-1 (SRC-1) specifically bound to serum response factor (SRF), as demonstrated by glutathione S-transferase pull down assays, and the yeast and mammalian two-hybrid tests. In mammalian cells, SRC-1 potentiated serum response element (SRE)-mediated transactivations in a dose-dependent manner. Coexpression of p300 synergistically enhanced this SRC-1-potentiated level of transactivations, consistent with the recent finding (Ramirez, S., Ali, S. A. S., Robin, P., Trouche, D., and Harel-Bellan, A. (1997) J. Biol. Chem. 272, 31016-31021) in which the p300 homologue CREB-binding protein was shown to be a transcription coactivator of SRF. Thus, we concluded that at least two distinct classes of coactivator molecules may cooperate to regulate SRF-dependent transactivations in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Binding Proteins / metabolism*
  • HeLa Cells
  • Histone Acetyltransferases
  • Humans
  • Nuclear Proteins / metabolism*
  • Nuclear Receptor Coactivator 1
  • Protein Binding
  • Serum Response Factor
  • Transcription Factors / metabolism*
  • Transcriptional Activation*
  • Transfection

Substances

  • DNA-Binding Proteins
  • Nuclear Proteins
  • Serum Response Factor
  • Transcription Factors
  • Histone Acetyltransferases
  • NCOA1 protein, human
  • Nuclear Receptor Coactivator 1