Homologous tyrosine phosphorylation sites in transformation-specific gene products of distinct avian sarcoma viruses

Neil, J. C. , Ghysdael, J., Vogt, P. K. and Smart, J. E. (1981) Homologous tyrosine phosphorylation sites in transformation-specific gene products of distinct avian sarcoma viruses. Nature, 291(5817), pp. 675-677. (doi: 10.1038/291675a0) (PMID:6264320)

Abstract

Three classes of avian sarcoma viruses have been defined recently (Table 1)1–5. Transformation-specific proteins of all three viral classes have associated tyrosine-specific protein kinase activity4–12. The protein kinase activity of Rous sarcoma viruses (RSV), representing class I, seems to be a property of the transformation-specific protein, pp60src, itself13 and seems to be essential for cellular transformation, as the activity is labile or absent in transformation mutants6,7,14,15. This connection between transformation-specific protein, enzyme activity and oncogenic cellular changes has yet to be established for the viruses of classes II and III, which code for polyproteins in which gag-derived and transformation-specific sequences are fused. We report here an analysis of the phosphorylation sites on the transformation-specific proteins encoded by RSV and the class III viruses which shows that, although there is no appreciable sequence relationship between large portions of these molecules, a tryptic peptide containing the phosphotyrosine seems to be identical in classes I and III.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Neil, Professor James
• Authors: Neil, J. C., Ghysdael, J., Vogt, P. K., and Smart, J. E.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity
• Journal Name: Nature
• Publisher: Nature Publishing Group
• ISSN: 0028-0836
• ISSN (Online): 1476-4687