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• W1667650047 abstract "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." @default.
• W1667650047 created "2016-06-24" @default.
• W1667650047 creator A5031408829 @default.
• W1667650047 creator A5065889841 @default.
• W1667650047 date "1984-07-01" @default.
• W1667650047 modified "2023-10-15" @default.
• W1667650047 title "Conditional inversion of the thermoresponse in Escherichia coli" @default.
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• W1667650047 doi "https://doi.org/10.1128/jb.159.1.360-367.1984" @default.
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