Choi C Y, Choi B H, Park G T, Rho H M
Department of Molecular Biology and Research Center for Cell Differentiation, Seoul National University, Seoul 151-742, Korea.
J Biol Chem. 1997 Jul 4;272(27):16934-9. doi: 10.1074/jbc.272.27.16934.
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.
