Indirect role of adenylate cyclase and cyclic AMP in chemotaxis to phosphotransferase system carbohydrates in Escherichia coli K-12.
Most strains of Escherichia coli K-12 lacking the enzyme adenylate cyclase showed normal chemotaxis toward carbohydrates taken up and phosphorylated by the phosphoenolpyruvate-dependent carbohydrate: phosphotransferase system. The normal reaction was observed even in the absence of externally added cyclic adenosine 3',5'-phosphate, provided that the enzyme II chemoreceptors and the flagella were synthesized. In the CA8306 series of strains, however, the cya-854 deletion abolished chemotaxis toward phosphotransferase system carbohydrates even though growth on and transport of these carbohydrates were not affected. This abnormal phenotype was due to the presence of a specific mutation in strain CA8306 which mapped in or close to the crp locus and apparently prevented expression of a hitherto unidentified molecule involved in enzyme II-mediated signal transduction. This molecule is neither a pts protein nor a cyclic adenosine 3',5'-phosphate-binding protein.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000483:Alleles; D002241:Carbohydrates; D002633:Chemotaxis; D000242:Cyclic AMP / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D005838:Genotype; D009154:Mutation; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D013045:Species Specificity
D002241:Carbohydrates; D000242:Cyclic AMP; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D000262:Adenylyl Cyclases