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(Received for publication, January 18, 1996, and in revised form, May 1, 1996)
From the Department of Pathology and Committee on Virology, Harvard
Medical School, Boston, Massachusetts 02115
The adenovirus E1A-associated protein p300
is a transcriptional cofactor that interacts with YY1 and mediates the
relief of YY1 transcriptional repression by E1A. These observations
raise the possibility that p300 may function as a bridging factor
between E1A and cellular transcription factors. Here we show that p300,
but not a mutant defective for binding to E1A, activated
cAMP-responsive element-binding protein/activating transcription factor
(CREB/ATF) binding site-mediated transcription in the presence of E1A.
Among proteins that can recognize the CREB/ATF site, CREB appeared to
be modulated by E1A in a p300 binding-dependent manner.
This effect of E1A was correlated with a specific physical interaction
between CREB and p300. These results suggest that p300 plays a crucial
role in mediating the functional interplay between E1A and certain
members of the CREB/ATF family. Two separate domains within p300 were
identified that are capable of activating transcription. One of the
domains interacted with the basal factor TFIIB, suggesting that p300
may function as a coactivator by making contacts with both
sequence-specific transcription factors and the basal transcriptional
machinery. This pivotal role of p300 may make it a prime target for
viral proteins such as E1A in programming the cellular transcription
machinery.
Volume 271, Number 30,
Issue of July 26, 1996
pp. 17666-17674
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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