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

Han Jong Kim, Jae-Hong Kim, Jae Woon Lee

Research output: Contribution to journalArticle

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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.

Original languageEnglish
Pages (from-to)28564-28567
Number of pages4
JournalJournal of Biological Chemistry
Volume273
Issue number44
DOIs
Publication statusPublished - 1998 Oct 30
Externally publishedYes

Fingerprint

Nuclear Receptor Coactivator 1
Serum Response Element
Serum Response Factor
Transcriptional Activation
CREB-Binding Protein
Two-Hybrid System Techniques
Songbirds
Transcription
Glutathione Transferase
Yeast
Assays
Cells
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations. / Kim, Han Jong; Kim, Jae-Hong; Lee, Jae Woon.

In: Journal of Biological Chemistry, Vol. 273, No. 44, 30.10.1998, p. 28564-28567.

Research output: Contribution to journalArticle

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