Interactions in vivo between IIIGlc of the phosphoenolpyruvate: sugar phosphotransferase system and the glycerol and maltose uptake systems of Salmonella typhimurium
Open Access
- 1 February 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 139 (1) , 29-34
- https://doi.org/10.1111/j.1432-1033.1984.tb07971.x
Abstract
Previous studies indicated that the ability of phosphoenolpyruvate:sugar phosphotransferase system (PTS) substrates to inhibit the uptake of glycerol or maltose in S. typhimurium is dependent on the relative cellular content of the PTS-sensitive uptake system and of the PTS protein glucose-specific factor III (IIIGlc). The present study confirms and extends those observations. The maltose and glycerol uptake systems were rendered (wholly or partially) insensitive to PTS inhibition by the presence of a 2nd PTS-sensitive uptake system (respectively, that for glycerol or maltose) and its substrate. The 2nd PTS-sensitive uptake system and its substrate were needed for this protective effect. Galactose and the galactose permease (a PTS-insensitive transport system) did not have any effect on PTS-mediated inhibition of the maltose uptake system. The protective effect of the 2nd PTS-sensitive uptake system and its substrate was counteracted by increasing the cellular levels of IIIGlc. Overproduction of IIIGlc in crr-plasmid-containing strains rendered the glycerol and maltose uptake systems hypersensitive to inhibition by PTS substrates. The results were interpreted on the basis of stoichiometric interaction between IIIGlc and a PTS-sensitive uptake system, in which the IIIGlc-transport-system complex is inactive. Competition between 2 PTS-sensitive transport system for formation of inactive complex with IIIGlc lowers the free intracellular concentration of IIIGlc resulting in a mutual protective effect against inhibition by IIIGlc.This publication has 29 references indexed in Scilit:
- Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: evidence for direct binding of the glucose-specific enzyme III to the lactose permease.Proceedings of the National Academy of Sciences, 1982
- Physical mechanism for regulation of phosphoenolpyruvate-dependent glucose transport activity in Escherichia coliBiochemistry, 1981
- Multiple methylation in processing of sensory signals during bacterial chemotaxis.Proceedings of the National Academy of Sciences, 1980
- Escherichia coli adenylate cyclase complex: regulation by the proton electrochemical gradient.Proceedings of the National Academy of Sciences, 1979
- Synthesis of Adenosine 3':5'-Cyclic Monophosphate in Salmonella typhimurium Growing in Continuous CultureJournal of General Microbiology, 1979
- The bacterial phosphoenolpyruvate: Sugar phosphotransferase systemBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1976
- Sugar transport. 2nducer exclusion and regulation of the melibiose, maltose, glycerol, and lactose transport systems by the phosphoenolpyruvate:sugar phosphotransferase system.Journal of Biological Chemistry, 1976
- A simple direct assay for cyclic amp in plasma and other biological samples using an improved competitive protein binding techniqueClinica Chimica Acta; International Journal of Clinical Chemistry, 1974
- Studies on the glucose-transport system in Escherichia coli with α-methylglucoside as substrateBiochimica et Biophysica Acta, 1963
- EFFECT OF METABOLIC ACTIVITY OF THE GLUCOSE PERMEASE OF BACTERIAL CELLSProceedings of the National Academy of Sciences, 1962