Synthesis, phosphorylation, and nuclear localization of human papillomavirus E7 protein in Schizosaccharomyces pombe

Gene. 1990 Sep 14;93(2):265-70. doi: 10.1016/0378-1119(90)90234-i.


The complete E7 protein-encoding open reading frame of human papillomavirus type 16 (HPV-16) was expressed in the fission yeast Schizosaccharomyces pombe, under the control of a cloned yeast promoter. The HPV-16 E7 protein synthesized in S. pombe is a 17-kDa phosphoprotein which is recognized by anti-E7 antibodies (raised in rabbits against E7 fusion protein produced in Escherichia coli). The mobility during sodium dodecyl sulfate-polyacrylamide-gel electrophoresis of native E7 phosphoprotein synthesized in S. pombe is identical to that of the E7 phosphoprotein immunoprecipitated from human CaSki cells. Immunofluorescence staining showed that HPV-16 E7 phosphoprotein is localized in the nuclei of transformed S. pombe. These results indicate that E7 protein synthesized by S. pombe is apparently indistinguishable from HPV-16 E7 protein synthesized in higher eukaryotic cells expressing genes of HPV-16, and also that the phosphorylated, nuclear HPV-16 E7 protein is synthesized in S. pombe in a form compatible with its biological activity.

MeSH terms

  • Animals
  • Base Sequence
  • Cell Nucleus / ultrastructure
  • Fluorescent Antibody Technique
  • Humans
  • Molecular Sequence Data
  • Oncogene Proteins, Viral / biosynthesis
  • Oncogene Proteins, Viral / genetics*
  • Open Reading Frames
  • Papillomaviridae / genetics
  • Phosphoproteins / biosynthesis
  • Phosphoproteins / genetics*
  • Phosphorylation
  • Promoter Regions, Genetic
  • Protein Biosynthesis
  • Rabbits
  • Schizosaccharomyces / genetics*
  • Schizosaccharomyces / ultrastructure
  • Transcription, Genetic


  • Oncogene Proteins, Viral
  • Phosphoproteins
  • oncogene protein E7, Human papillomavirus type 8