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(Received for publication, February 24, 1997, and in revised form, April 24, 1997)
From the Department of Molecular Biology and Research Center for
Cell Differentiation, Seoul National University,
Seoul 151-742, Korea
The hepatitis B viral X promoter is known to be
positively autoregulated by its own HBx protein, which also interacts
with many cellular regulatory proteins. We investigated the effect of
activating transcription factor 2 (ATF2) on the activity of the X
promoter. Cotransfection of the ATF2 expression vector with a X
promoter-chloramphenicol acetyltransferase plasmid repressed the X
promoter activity in HepG2 cells. HBx activated activating protein 1 (AP-1)-mediated transcription through the hepatitis B virus E element
by 35-fold, while its activation activity was inhibited in the presence
of ATF2, suggesting that ATF2 inhibited the autoactivation of X
promoter by HBx and basal transcription mediated by AP-1. Since the
binding sites of AP-1 and ATF2 in the hepatitis B virus E element
overlap, the repression of X promoter activity by ATF2 is exerted by
the competition for the AP-1 binding site and the formation of the
ATF2-Jun heterodimer as in the case of the consensus AP-1 element.
However, the small X promoter had a ATF2 binding site and was activated
by ATF2. These results suggest that the syntheses of X proteins are
differentially regulated by ATF2.
Volume 272, Number 27,
Issue of July 4, 1997
pp. 16934-16939
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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