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Vol. 12, No. 3, pp. 331-342, February 1, 1998
Department of Biology and Center for Molecular Genetics,
University of California, San Diego,
La Jolla, California 92093-0347 USA
Estrogen- and antiestrogen-regulated, AF-2-dependent
transcriptional activation by purified full-length human estrogen
receptor (ER) was carried out with chromatin templates in vitro. With
this system, the ability of purified human p300 to function as a
transcriptional coactivator was examined. In the absence of
ligand-activated ER, p300 was found to have little effect (less than
twofold increase) on transcription, whereas, in contrast, p300 was
observed to act synergistically with ligand-activated ER to enhance
transcription. When transcription was limited to a single round, p300
and ER were found to enhance the efficiency of transcription initiation in a cooperative manner. On the other hand, when transcription reinitiation was allowed to occur, ER, but not p300, was able to
increase the number of rounds of transcription. These results suggest a
two-stroke mechanism for transcriptional activation by ligand-activated
ER and p300. In the first stroke, ER and p300 function cooperatively to
increase the efficiency of productive transcription initiation. In the
second stroke, ER promotes the reassembly of the transcription
preinitiation complex. Therefore, ER exhibits distinct, dual functions
in transcription initiation and reinitiation.
[Key Words: RNA polymerase II; in vitro transcription; estrogen receptor; p300; CBP; coactivator; nuclear receptors]
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