In vivo phosphorylation of Saccharomyces cerevisiae ribosomal protein S10 by cyclic-AMP-dependent protein kinase.
Using wild-type Saccharomyces cerevisiae strains and mutants which are defective in the regulatory subunit of cyclic-AMP-dependent protein kinase (bcy1) and phosphoprotein phosphatase activity (ppd1), we demonstrated that a cyclic-AMP-dependent protein kinase phosphorylated the S. cerevisiae ribosomal protein S10 in vivo. S10 was not dephosphorylated in bcy1 or ppd1 mutants after heat shock. The phosphorylated forms of S10 were diminished during the stationary phase in bcy1 and ppd1 mutants as well as in wild-type cells.
D002453:Cell Cycle; D000242:Cyclic AMP / Q000502:physiology; D006358:Hot Temperature; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000648:ultrastructure
D010750:Phosphoproteins; D012269:Ribosomal Proteins; D000242:Cyclic AMP; D011494:Protein Kinases