Two different protein kinase activities phosphorylate Ras2 protein in Saccharomyces cerevisiae.
In this report, we show that Ras2 protein in the yeast Saccharomyces cerevisiae is phosphorylated in vivo by protein kinase(s) and the phosphorylation is stable. Ras2 protein is phosphorylated by cAMP dependent protein kinase and by an additional protein kinase activity which is independent of cAMP levels.
Sreenath
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Laboratory of Molecular Virology, National Cancer Institute, Bethesda, MD 20892.
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Ahmed
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D000262:Adenylyl Cyclases / Q000235:genetics / Q000378:metabolism; D000242:Cyclic AMP / Q000378:metabolism / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000378:metabolism*; D006358:Hot Temperature; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D009154:Mutation; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D018631:ras Proteins
D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; C489015:RAS2 protein, S cerevisiae; D018631:ras Proteins; D000262:Adenylyl Cyclases