In vitro analysis of the two-component system MtrB-MtrA from Corynebacterium glutamicum

J Bacteriol. 2007 May;189(9):3645-9. doi: 10.1128/JB.01920-06. Epub 2007 Feb 9.

Abstract

The two-component system MtrBA is involved in the osmostress response of Corynebacterium glutamicum. MtrB was reconstituted in a functionally active form in liposomes and showed autophosphorylation and phosphatase activity. In proteoliposomes, MtrB activity was stimulated by monovalent cations used by many osmosensors for the detection of hypertonicity. Although MtrB was activated by monovalent cations, they lead in vitro to a general stabilization of histidine kinases and do not represent the stimulus for MtrB to sense hyperosmotic stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism*
  • Adaptation, Physiological
  • Bacterial Proteins / drug effects
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cations, Monovalent / pharmacology
  • Corynebacterium glutamicum / genetics
  • Corynebacterium glutamicum / physiology*
  • Enzyme Activators / pharmacology
  • Liposomes
  • Osmotic Pressure
  • Phosphoric Monoester Hydrolases / drug effects
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphorylation
  • RNA-Binding Proteins / drug effects
  • RNA-Binding Proteins / metabolism*
  • Signal Transduction
  • Transcription Factors / drug effects
  • Transcription Factors / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Cations, Monovalent
  • Enzyme Activators
  • Liposomes
  • MtrA protein, Bacteria
  • MtrB protein, Bacteria
  • RNA-Binding Proteins
  • Transcription Factors
  • Phosphoric Monoester Hydrolases