Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism

Proc Natl Acad Sci U S A. 1988 Aug;85(15):5492-6. doi: 10.1073/pnas.85.15.5492.

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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins*
  • Chemotactic Factors / genetics*
  • Chemotaxis*
  • Chromatography, Gel
  • Cross Reactions
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins
  • Histidine Kinase
  • Membrane Proteins / genetics*
  • Methyl-Accepting Chemotaxis Proteins
  • Mutation
  • Nitrogen / metabolism*
  • Phenotype
  • Phosphates / metabolism
  • Phosphorylation
  • Promoter Regions, Genetic
  • Salmonella typhimurium / genetics
  • Salmonella typhimurium / metabolism
  • Transcription, Genetic*
  • Transduction, Genetic

Substances

  • Bacterial Proteins
  • Chemotactic Factors
  • Escherichia coli Proteins
  • Membrane Proteins
  • Methyl-Accepting Chemotaxis Proteins
  • Phosphates
  • cheY protein, E coli
  • Histidine Kinase
  • cheA protein, E coli
  • Nitrogen