Ishido S, Muramatsu S, Fujita T, Iwanaga Y, Tong W Y, Katayama Y, Itoh M, Hotta H
Department of Microbiology, Kobe University School of Medicine, Chuo-ku, Hyogo, Japan.
Biochem Biophys Res Commun. 1997 Jan 13;230(2):431-6. doi: 10.1006/bbrc.1996.5980.
By using vaccinia virus-T7 hybrid expression system, subcellular localization of the NS3 protein of hepatitis C virus was studied. Full-size NS3 (NS3F) and a carboxy-terminally truncated form (NS3 deltaC) were localized in the cytoplasm and the nucleus when expressed alone. However, NS3F and NS3 deltaC, but not amino- and carboxy-terminally truncated form (NS3 deltaN deltaC), were each co-localized with wild-type p53 almost exclusively in the nucleus upon co-expression. The wild-type p53-induced nuclear accumulation of NS3F was inhibited only partially by NS4A. When co-expressed with mutant-type p53, NS3F and NS3 deltaC were each co-localized with it exclusively in the cytoplasm. Taken together, the present results suggest that wild-type p53 enhances nuclear accumulation of NS3F and NS3 deltaC through the involvement of their amino-terminal sequences even in the presence of NS4A, and that mutant-type p53 inhibits their nuclear, and enhances their cytoplasmic, accumulation.
