Multiple kinetic states for the flagellar motor switch.
By means of a computerized video processing system, the flagellar motors of Escherichia coli were shown to have multiple kinetic states for each rotational direction. High-resolution analysis of flagellar motors revealed new kinetic states both in wild-type cells and in a strain deleted of other signal-transducing genes to which CheY had been introduced. This strain, RP1091, retained residual kinase activity that could phosphorylate CheY, complicating the biochemical identification of certain kinetic states. The behavioral effect of CheY on single flagellar motors was ultrasensitive, with an apparent Hill coefficient of 5.5 +/- 1.9 (SD) and a half-maximal effect at 10.1 +/- 0.5 (SD) microM CheY. Based on the CheY concentration dependence, a two-state model is clearly excluded, even for the simpler system of CheY-induced rotational reversals in the deletion strain. The data are best described by a four-state model, with two clockwise and two counterclockwise states.
Kuo
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SC
Department of Biochemistry, University of California, Berkeley 94720.
Koshland
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DE
D001426:Bacterial Proteins; D002630:Chemotactic Factors / Q000235:genetics*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins; D005407:Flagella / Q000502:physiology*; D005798:Genes, Bacterial; D007700:Kinetics; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D008962:Models, Theoretical; D010766:Phosphorylation; D010957:Plasmids; D015183:Restriction Mapping; D013997:Time Factors; D014741:Video Recording / Q000379:methods
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli