Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis.
Six cytoplasmic che gene products are required for signal transduction in bacterial chemotaxis, but the nature of their biochemical interactions is not known. We show that in vitro the CheA protein becomes autophosphorylated in the presence of ATP. In addition, the phosphate group on CheA can be rapidly transferred to CheB, a protein involved in adaptation to stimuli, or to CheY, a protein involved in the excitation response. The phosphorylation of CheB and CheY is transient; they readily dephosphorylate. We have also found that CheZ, a protein that appears to antagonize CheY function in vivo, accelerates the hydrolysis of the phosphate on CheY. These results suggest that signal transduction in bacterial chemotaxis may involve the flow of phosphate through a cascade of phosphorylated protein intermediates.
Hess
J F
JF
Division of Biology, California Institute of Technology, Pasadena 91125.
Oosawa
K
K
Kaplan
N
N
Simon
M I
MI
D001426:Bacterial Proteins / Q000378:metabolism*; D002630:Chemotactic Factors / Q000378:metabolism*; D002633:Chemotaxis; D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins; D000071677:Histidine Kinase; D007700:Kinetics; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D010766:Phosphorylation
D001426:Bacterial Proteins; D002630:Chemotactic Factors; 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