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Ishido, S. et al.

Wild-type, but not mutant-type, p53 enhances nuclear accumulation of the NS3 protein of hepatitis C virus.

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.[1]

References

Wild-type, but not mutant-type, p53 enhances nuclear accumulation of the NS3 protein of hepatitis C virus. Ishido, S., Muramatsu, S., Fujita, T., Iwanaga, Y., Tong, W.Y., Katayama, Y., Itoh, M., Hotta, H. Biochem. Biophys. Res. Commun. (1997) [Pubmed]

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