Demethylation of bacterial chemoreceptors is inhibited by attractant stimuli in the complete absence of the regulatory domain of the demethylating enzyme

Alain Borczuk, Ariane Staub, Jeff Stock

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

The CheB methylesterase catalyzes the demethylation of membrane receptors during chemotaxis in Salmonella typhimurium. The kinetic properties of the full length product of the cheB gene are compared to those of the isolated C-terminal catalytic domain. The fragment has at least a 15-fold higher specific activity than the intact protein. In intact cells receptor demethylation is inhibited by attractants such as L-aspartate. We show here that both forms of the enzyme are similarly inhibited in vitro. Thus, the C-terminal catalytic domain of the CheB protein is sufficient for this aspect of esterase regulation. Inhibition by attractants appears to be caused by changes in receptor conformation rather than by changes in the activity of the demethylating enzyme.

Original languageEnglish (US)
Pages (from-to)918-923
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume141
Issue number3
DOIs
StatePublished - Dec 30 1986

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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