Abstract
We demonstrate by using purified bacterial components that the protein kinases that regulate chemotaxis and transcription of nitrogen-regulated genes, CheA and NRII, respectively, have cross-specificities: CheA can phosphorylate the Ntr transcription factor NRI and thereby activate transcription from the nitrogen-regulated glnA promoter, and NRII can phosphorylate CheY. In addition, we find that a high intracellular concentration of a highly active mutant form of NRII can suppress the smooth-swimming phenotype of a cheA mutant. These results argue strongly that sensory transduction in the Ntr and Che systems involves a common protein phosphotransfer mechanism.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins*
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Chemotactic Factors / genetics*
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Chemotaxis*
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Chromatography, Gel
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Cross Reactions
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins
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Histidine Kinase
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Membrane Proteins / genetics*
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Methyl-Accepting Chemotaxis Proteins
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Mutation
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Nitrogen / metabolism*
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Phenotype
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Phosphates / metabolism
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Phosphorylation
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Promoter Regions, Genetic
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Salmonella typhimurium / genetics
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Salmonella typhimurium / metabolism
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Transcription, Genetic*
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Transduction, Genetic
Substances
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Bacterial Proteins
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Chemotactic Factors
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Escherichia coli Proteins
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Membrane Proteins
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Methyl-Accepting Chemotaxis Proteins
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Phosphates
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cheY protein, E coli
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Histidine Kinase
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cheA protein, E coli
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Nitrogen