title: Change in direction of flagellar rotation in Escherichia coli mediated by acetate kinase.
abstract: Strains of Escherichia coli lacking all cytoplasmic chemotaxis proteins except CheY swim smoothly under most conditions. However, they tumble when exposed to acetate. Acetate coenzyme A synthetase (EC 6.2.1.1) was thought to be essential for this response. New evidence suggests that the tumbling is mediated instead by acetate kinase (EC 2.7.2.1), which might phosphorylate CheY via acetyl phosphate. In strains that were wild type for chemotaxis, neither acetate coenzyme A synthetase, acetate kinase, nor phosphotransacetylase (EC 2.3.1.8) (and thus acetyl phosphate) was required for responses to aspartate, serine, or sugars sensed by the phosphotransferase system. Thus, acetate-induced tumbling does not appear to play an essential role in chemotaxis in wild-type cells.
authors.affiliation: Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.
authors.forename: F E
authors.initials: FE
authors.lastname: Dailey
authors.forename: H C
authors.initials: HC
authors.lastname: Berg
mesh_terms: D000084:Acetate Kinase / Q000378:metabolism*; D000106:Acetate-CoA Ligase / Q000378:metabolism; D001426:Bacterial Proteins; D002465:Cell Movement / Q000502:physiology*; D002633:Chemotaxis / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D010709:Phosphate Acetyltransferase / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli; D010709:Phosphate Acetyltransferase; D000084:Acetate Kinase; D000106:Acetate-CoA Ligase