In vitro transformation with Rous sarcoma virus and the pp60src-associated protein kinase.
Fifteen transformation defective sensitive mutants of Rous sarcoma virus have been investigated to see if the expression of the pp60src-associated protein kinase activity correlated with other parameters of transformation such as altered growth control, morphological changes, increased hexose transport, and increased plasminogen activator protease synthesis. The expression of a protein kinase activity paralleled or preceded the onset of other parameters of transformation with but one exception: altered control of cell growth. The stability of the pp60src molecule in mutant-infected cells at the nonpermissive temperature was investigated with the finding that mutant pp60src did not show an increased turnover at the nonpermissive temperature as compared to wild type virus pp60src. Furthermore, it could be shown that pre-existing pp60src in mutant-infected cells maintained at the non-permissive temperature became activated after temperature shift to the permissive temperature. Temperature shift performed under conditions of inhibition of new protein synthesis with cycloheximide, puromycin, or emetine was followed by greatly increased protein kinase activity, and a parallel phosphorylation of pp60src itself in tyrosine residues. Morphological features of transformation could be demonstrated likewise under conditions of inhibition of protein synthesis.
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000201:enzymology* / Q000235:genetics; D002472:Cell Transformation, Viral; D009154:Mutation; D015688:Oncogene Protein pp60(v-src); D010641:Phenotype; D011494:Protein Kinases / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics*
D014764:Viral Proteins; D011494:Protein Kinases; D015688:Oncogene Protein pp60(v-src)