Conditional inversion of the thermoresponse in Escherichia coli.
Mutants in Escherichia coli having defects in one of the methyl-accepting chemotaxis proteins, Tsr protein, which is the chemoreceptor and transducer for L-serine, showed a reduced but similar type of thermoresponse compared with wild-type strains; the cells showed smooth swimming upon temperature increase and tumbling upon temperature decrease. However, when the mutant cells were adapted to attractants such as L-aspartate and maltose, which are specific to another methyl-accepting chemotaxis protein, Tar protein, the direction of the thermoresponse was found to be inverted; a temperature increase induced tumbling and a temperature decrease induced smooth swimming. Consistent with this, the mutant cells showed inverted changes in the methylation level of Tar protein upon temperature changes. Wild-type strains but not Tar protein-deficient mutants exhibited the inverted thermoresponse when the cells were simultaneously adapted to L-aspartate and L-serine, indicating that Tar protein has a key role in the inversion of the thermoresponse. Thus, besides Tsr protein, Tar protein has a certain role in thermoreception. A simple model for thermoreception and inversion of the thermoresponse is also discussed.
D001426:Bacterial Proteins; D002465:Cell Movement; D002630:Chemotactic Factors / Q000378:metabolism; D002633:Chemotaxis; D003470:Culture Media; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development*; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D008745:Methylation; D009154:Mutation; D013696:Temperature
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D003470:Culture Media; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607604:tsr protein, E coli