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J Biol Chem, Vol. 273, Issue 44, 28564-28567, October 30, 1998
,¶
From the 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.
College of Pharmacy and ¶ Hormone
Research Center, Chonnam National University, Kwangju 500-757, Korea
and the § Institute of Environmental and Life Sciences,
Hallym University, Chuncheon 200-702, Korea
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