Characterization of a nuclear localization sequence in the polyomavirus capsid protein VP1

Virology. 1991 Nov;185(1):513-8. doi: 10.1016/0042-6822(91)90811-o.

Abstract

Expression of VP1-beta-galactosidase fusion proteins in the yeast Saccharomyces cerevisiae was used to identify a domain of the polyomavirus VP1 capsid protein which targets this protein to the nucleus. Fusion of the first 17 amino acids of VP1 to beta-galactosidase was sufficient for nuclear localization, whereas fusion of the first 12 amino acids gave a "mixed" cytoplasmic-nuclear phenotype. Mutation of a putative targeting sequence MAPKR(5)K from R to S changed the localization of a 21 amino acid fusion protein from the nucleus to cytoplasm. These results define a nuclear location signal in the amino terminus of polyomavirus VP1 and separate this function from the high-affinity DNA binding function previously defined for this region.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Base Sequence
  • Capsid / analysis
  • Capsid / genetics*
  • Capsid / metabolism
  • Capsid Proteins*
  • Cell Line
  • Cell Nucleus / metabolism*
  • Genetic Vectors
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides
  • Plasmids
  • Polyomavirus / genetics*
  • Recombinant Fusion Proteins / analysis
  • Recombinant Fusion Proteins / metabolism
  • Restriction Mapping
  • Saccharomyces cerevisiae / genetics
  • beta-Galactosidase / analysis
  • beta-Galactosidase / genetics
  • beta-Galactosidase / metabolism

Substances

  • Capsid Proteins
  • Oligodeoxyribonucleotides
  • Recombinant Fusion Proteins
  • VP1 protein, polyomavirus
  • beta-Galactosidase