Herpesvirus saimiri oncogene STP-C488 encodes a phosphoprotein.
The STP-C488 open reading frame of herpesvirus saimiri encodes an oncoprotein that has transforming and tumor-inducing activities independent of the rest of the herpesvirus genome. STP-C488 protein has an unusual, membrane-associated, fibrous structure and is located primarily in perinuclear compartments. We now report that STP-C488 is phosphorylated in vivo. The phosphorylated form, which accounted for about 15% of STP-C488 in transformed cells, migrated slightly more slowly through sodium dodecyl sulfate-polyacrylamide gels than unphosphorylated STP-C488. A serine residue near the amino terminus was shown to be the site of phosphorylation. However, phosphorylation was not required for transformation of Rat-1 cells by STP-C488.
Jung
J U
JU
New England Regional Primate Research Center, Harvard Medical School, Southborough, Massachusetts 01772-9102.
Desrosiers
R C
RC
D000818:Animals; D002472:Cell Transformation, Viral; D002478:Cells, Cultured; D005814:Genes, Viral; D006567:Herpesvirus 2, Saimiriine / Q000235:genetics*; D066298:In Vitro Techniques; D008970:Molecular Weight; D009856:Oncogene Proteins, Viral / Q000737:chemistry* / Q000235:genetics; D009857:Oncogenes; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics; D010768:Phosphoserine / Q000737:chemistry; D051381:Rats; D015678:Viral Structural Proteins / Q000235:genetics
D009856:Oncogene Proteins, Viral; D010750:Phosphoproteins; C072817:STP-C488 protein, Herpesvirus saimiri; D015678:Viral Structural Proteins; D010768:Phosphoserine