title: Wild-type, but not mutant-type, p53 enhances nuclear accumulation of the NS3 protein of hepatitis C virus.
abstract: 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.
authors.affiliation: Department of Microbiology, Kobe University School of Medicine, Chuo-ku, Hyogo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Ishido
authors.forename: S
authors.initials: S
authors.lastname: Muramatsu
authors.forename: T
authors.initials: T
authors.lastname: Fujita
authors.forename: Y
authors.initials: Y
authors.lastname: Iwanaga
authors.forename: W Y
authors.initials: WY
authors.lastname: Tong
authors.forename: Y
authors.initials: Y
authors.lastname: Katayama
authors.forename: M
authors.initials: M
authors.lastname: Itoh
authors.forename: H
authors.initials: H
authors.lastname: Hotta
mesh_terms: D001483:Base Sequence; D002467:Cell Nucleus / Q000378:metabolism*; D017931:DNA Primers; D019084:Fluorescent Antibody Technique, Indirect; D005822:Genetic Vectors; D006367:HeLa Cells; D016174:Hepacivirus / Q000502:physiology*; D006801:Humans; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000032:analysis / Q000096:biosynthesis / Q000378:metabolism; D017384:Sequence Deletion; D012697:Serine Endopeptidases / Q000096:biosynthesis; D014162:Transfection; D016159:Tumor Suppressor Protein p53 / Q000235:genetics / Q000378:metabolism*; D014616:Vaccinia virus; D017361:Viral Nonstructural Proteins / Q000032:analysis / Q000096:biosynthesis*; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases
chemical_list: D017931:DNA Primers; D011994:Recombinant Proteins; D012697:Serine Endopeptidases; D016159:Tumor Suppressor Protein p53; D017361:Viral Nonstructural Proteins; C084422:NS3 protein, hepatitis C virus; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases