Protein phosphorylation is involved in bacterial chemotaxis.
The nature of the biochemical signal that is involved in the excitation response in bacterial chemotaxis is not known. However, ATP is required for chemotaxis. We have purified all of the proteins involved in signal transduction and show that the product of the cheA gene is rapidly autophosphorylated, while some mutant CheA proteins cannot be phosphorylated. The presence of stoichiometric levels of two other purified components in the chemotaxis system, the CheY and CheZ proteins, induces dephosphorylation. We suggest that the phosphorylation of CheA by ATP plays a central role in signal transduction in chemotaxis.
Hess
J F
JF
Division of Biology, California Institute of Technology, Pasadena 91125.
Oosawa
K
K
Matsumura
P
P
Simon
M I
MI
D001426:Bacterial Proteins; D002633:Chemotaxis; D004926:Escherichia coli / Q000235:genetics* / Q000502:physiology; D029968:Escherichia coli Proteins; D005796:Genes; D005798:Genes, Bacterial; D000071677:Histidine Kinase; D007700:Kinetics; D008565:Membrane Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D010766:Phosphorylation
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli; D000071677:Histidine Kinase; C000607608:cheA protein, E coli