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J Biol Chem, Vol. 273, Issue 27, 16651-16654, July 3, 1998
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From the Steroid receptor coactivator-1 (SRC-1)
specifically bound to the transcription factor AP-1 subunits c-Jun and
c-Fos, as demonstrated by the yeast two-hybrid tests and glutathione
S-transferase pull down assays. The c-Jun and c-Fos binding
sites were localized to the C-terminal subregion of SRC-1 (amino acids
1101-1441) that encompasses the previously described histone
acetyltransferase and receptor-binding domains. In mammalian cells,
SRC-1, similar to the previous results with CBP-p300 (Arias, J.,
Alberts, A. S., Brindle, P., Claret, F. X., Smeal, T., Karin,
M., Feramisco, J., and Montminy, M. (1994) Nature 370, 226-229; Bannister, A. J., and Kouzarides, T. (1995) EMBO
J. 14, 4758-4762), potentiated the AP-1-mediated
transactivations in a dose-dependent manner and derepressed the
mutual inhibitions between nuclear receptors and AP-1. Furthermore,
coexpression of p300 further enhanced this SRC-1-potentiated level of
transactivations. Thus, we concluded that at least two distinct
coactivator molecules may cooperate to regulate
AP-1-dependent transactivations and mediate transrepression between AP-1 and nuclear receptors in vivo.
College of Pharmacy, the
§ Department of Biology, the ¶ Hormone Research Center,
and the Department of Microbiology, Chonnam National University,
Kwangju 500-757, Korea
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