Characterization of the presumptive phosphorylation sites of the Bacillus subtilis glucose permease by site-directed mutagenesis: implication in glucose transport and catabolite repression

FEMS Microbiol Lett. 1997 Nov 15;156(2):233-8. doi: 10.1111/j.1574-6968.1997.tb12733.x.

Abstract

Bacillus subtilis utilizes glucose as the preferred source of carbon and energy. Glucose is transported and concomitantly phosphorylated by the glucose permease (PtsG) of the phosphoenolpyruvate:sugar phosphotransferase system. The phosphate is transferred from enzyme I via HPr and domains IIA and IIB of the glucose permease to the sugar. In this study mutants affected in the putative phosphorylation sites of glucose permease were constructed and the effect on sugar transport and glucose repression tested. Phosphorylation of both domains IIAGlc and IIBGlc is required for efficient glucose transport and repression of beta-xylosidase and the bglPH operon.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / enzymology
  • Bacillus subtilis / genetics*
  • Carbon / metabolism
  • Genotype
  • Glucose / pharmacokinetics*
  • Mutagenesis, Site-Directed / physiology
  • Operon / physiology
  • Phosphoenolpyruvate Sugar Phosphotransferase System / genetics*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
  • Phosphorylation
  • Point Mutation
  • Xylosidases / metabolism

Substances

  • Carbon
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphoenolpyruvate-glucose phosphotransferase
  • Xylosidases
  • exo-1,4-beta-D-xylosidase
  • Glucose