Sensory transduction in bacterial chemotaxis involves phosphotransfer between Che proteins.
The CheA protein of the Salmonella typhimurium chemotaxis system is phosphorylated by ATP. Phospho-CheA transfers its phosphoryl group to a second chemotaxis protein, CheY. Unlike phospho-CheA, phospho-CheY is relatively unstable, rapidly decaying to phosphate and CheY. We propose that phosphorylation of CheY may play a role in its function as a tumble regulator to control motor behavior in response to attractant and repellent stimuli.
Wylie
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Department of Molecular Biology, Princeton University, NJ 08544.
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Wong
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D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins; D002630:Chemotactic Factors / Q000378:metabolism*; D002633:Chemotaxis; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D010766:Phosphorylation; D012486:Salmonella typhimurium / Q000502:physiology*
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D000255:Adenosine Triphosphate