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(Received for publication, January 27, 1997, and in revised form, April 25, 1997)
From the Molecular Cardiology Laboratory, SRI International, Menlo
Park, California 94125
Adenovirus E1A oncoproteins inhibit
muscle-specific gene expression and myogenic differentiation by
suppressing the transcriptional activating functions of basic
helix-loop-helix proteins. As one approach to identifying
cardiac-specific gene regulatory proteins, we analyzed the functional
regions of E1A proteins that are required for muscle gene repression in
cardiac cells. Myocyte-specific promoters, including the
Volume 272, Number 33,
Issue of August 15, 1997
pp. 20584-20594
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
-actins and
-myosin heavy chain, were selectively and potently inhibited
(>90%) by E1A, while the ubiquitously expressed 
-actin promoter
was only partially (~30%) repressed; endogenous gene expression was
also affected. Distinct E1A protein binding sites mediated repression
of muscle-specific and ubiquitous actin promoters. E1A-mediated
inhibition of -actin required both an intact binding site for the
tumor repressor proteins pRb and p107 and a second E1A domain (residues
15-35). In contrast, cardiac-specific promoter repression required the
E1A amino-terminal residues 2-36. The proximal skeletal actin promoter
(3
to base pair 
153) was a target for repression by E1A. Although
E1A binding to p300 was not required for inhibition of either promoter,
co-expression of p300 partially reversed E1A-mediated transcriptional
repression. We conclude that cardiac-specific and general promoter
inhibition by E1A occurs by distinct mechanisms and that
cardiac-specific gene expression is modulated by cellular factors
interacting with the E1A p300/CBP-binding domain.
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