Chemosensory and thermosensory excitation in adaptation-deficient mutants of Escherichia coli

J Bacteriol. 1984 Jul;159(1):368-74. doi: 10.1128/jb.159.1.368-374.1984.

Abstract

Methyl-accepting chemotaxis protein-methyltransferase-deficient mutants, cheR mutants, of Escherichia coli showed a tumble response to repellents only at low temperatures, and the resultant tumbling lasted unless the condition was changed. The swimming pattern of the repellent-treated cells was different at different temperatures, indicating that the absolute temperature is a determinant of the tumbling frequency of those cells. The tumbling of those cells was also suppressed by the addition of attractants. Under a suitable repellent concentration, the tumbling frequency of the cells was found to be simply determined by the ligand occupancy of chemoreceptors for many attractants. In a methyl-accepting chemotaxis protein-methylesterase-deficient mutant, a cheB deletion mutant, the tumbling frequency was also determined by receptor occupancy of some attractants. These results indicate that in the adaptation-deficient mutants, sensory signals are produced in proportion to the amount of ligand-bound or of thermally altered receptors and transmitted to the flagellar motors without any modification. Thus, it is concluded that the adaptation system, namely, the methylation-demethylation system of methyl-accepting chemotaxis proteins, is not concerned with the step of chemosensory or thermosensory excitation. A simple model is proposed to explain how the swimming pattern of the adaptation-deficient mutants is determined.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Cell Movement
  • Chemotactic Factors / genetics*
  • Chemotaxis*
  • Escherichia coli / genetics
  • Escherichia coli / growth & development*
  • Membrane Proteins / genetics*
  • Methyl-Accepting Chemotaxis Proteins
  • Mutation*
  • Protein Methyltransferases / genetics*
  • Species Specificity
  • Temperature

Substances

  • Bacterial Proteins
  • Chemotactic Factors
  • Membrane Proteins
  • Methyl-Accepting Chemotaxis Proteins
  • Protein Methyltransferases