Evidence for protein kinase activities in the prokaryote Salmonella typhimurium.
Evidence for phosphorylation of proteins by protein kinases has been found in Salmonella typhimurium despite previous indications that protein kinase action is absent in prokaryotes. At least four proteins have been found to be phosphorylated. Serine and threonine phosphates have been isolated from acid hydrolysates of these proteins after in vivo and in vitro labeling. The kinases do not phosphorylate histones, casein, or phosvitin. It would appear that phosphorylation as a regulatory control exists in prokaryotes.
D000596:Amino Acids / Q000032:analysis; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000201:enzymology*
D000596:Amino Acids; D011494:Protein Kinases