The transforming protein of Moloney murine sarcoma virus is a soluble cytoplasmic protein.
The transforming gene, v-mos, of Moloney murine sarcoma virus (M-MuSV) encodes a 37,000-dalton phosphoprotein, p37mos. Since the biochemical function of this protein is unknown, we have determined the subcellular location of p37mos in M-MuSV 124-transformed cells. Using two different methods of cell lysis and fractionation, we found that newly synthesized as well as mature p37mos is a soluble cytoplasmic protein. In agreement with these results, immunofluorescent staining of cells acutely infected with M-MuSV 124, using an antiserum directed against a synthetic v-mos peptide, produced a diffuse cytoplasmic pattern. Gel filtration experiments and glycerol gradient sedimentation analysis suggest that the bulk of p37mos exists as a monomer and is not involved in a specific association with other cellular proteins. These properties of p37mos are different from those of other characterized retroviral transforming proteins.
D002451:Cell Compartmentation; D002472:Cell Transformation, Viral; D003593:Cytoplasm / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D008979:Moloney murine leukemia virus / Q000235:genetics*; D009857:Oncogenes; D012995:Solubility; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism
D014764:Viral Proteins