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(Received for publication, October 19, 1995; and in revised form, January
8, 1996) Human p300 protein is a cellular target of adenoviral E1A
oncoprotein and a potential transcriptional coactivator. Both p300 and
Rb family protein-binding regions of E1A are required for the
repression of muscle gene expression, which is regulated by MyoD family
transactivators. This implies that p300 is involved in MyoD-dependent
transactivation. We show that the repression of MyoD-mediated E box
(MyoD consensus) reporter activity by E1A is correlated with its
interaction with p300, indicating that p300 participates in
MyoD-dependent transactivation. In addition, p300 is able to interact
both in vivo and in vitro with MyoD through a portion
at the carboxyl-terminal cysteine/histidine-rich domain and associates
with the components of the basal transcriptional complex through its
two separate transactivation domains at the amino and carboxyl termini.
Consistent with its role as a coactivator, p300 potentiates
MyoD-activated transcription.
Volume 271,
Number 15,
Issue of April 12, 1996 pp. 9009-9013
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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