title: Sensory transduction in bacterial chemotaxis involves phosphotransfer between Che proteins.
abstract: 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.
authors.affiliation: Department of Molecular Biology, Princeton University, NJ 08544.
authors.forename: D
authors.initials: D
authors.lastname: Wylie
authors.forename: A
authors.initials: A
authors.lastname: Stock
authors.forename: C Y
authors.initials: CY
authors.lastname: Wong
authors.forename: J
authors.initials: J
authors.lastname: Stock
mesh_terms: 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*
chemical_list: D001426:Bacterial Proteins; D002630:Chemotactic Factors; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D000255:Adenosine Triphosphate