Regulation of glycerol and maltose uptake by the IIAGlc-like domain of IINag of the phosphotransferase system inSalmonella typhimurium LT2

Vlag, Johan van der; Postma, Pieter W.

doi:10.1007/bf02190806

Cited by 13 publications

(10 citation statements)

References 30 publications

(19 reference statements)

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“…Although glycerol is not transported by the PTS, mutants of gram-positive and gram-negative bacteria defective in one of (166,676,899). A mechanism completely different from that operating in E. coli and S. enterica serovar Typhimurium seems to control glycerol metabolism in most low-GϩC gram-positive bacteria.…”

Section: Regulation Of Glycerol Kinase By Pϳhis-hpr-mediated Phosphormentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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Section: Regulation Of Glycerol Kinase By Pϳhis-hpr-mediated Phosphormentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

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“…The presence of 1 mg/ml EIIA Glc of E. coli inhibited E. coli glycerol kinase activity about 3.5-fold (12). The S. typhimurium EIIA Nag domain which forms the C-terminal domain of the enzyme IICBA specific for N-acetylglucosamine and which strongly resembles EIIA Glc was also found to be able to inhibit S. typhimurium glycerol kinase activity similar to EIIA Glc (40). However, neither E. coli EIIA Glc at concentrations up to 2 mg/ml nor B. subtilis EIIA Glc domain at concentrations up to 0.7 mg/ml exerted an inhibitory effect on glycerol kinase of E. casseliflavus (data not shown).…”

Section: Effect Of Fbp and Eiiamentioning

confidence: 89%

Cloning and Sequencing of two Enterococcal glpK Genes and Regulation of the Encoded Glycerol Kinases by Phosphoenolpyruvate-dependent, Phosphotransferase System-catalyzed Phosphorylation of a Single Histidyl Residue

Charrier

Buckley

Parsonage

et al. 1997

Journal of Biological Chemistry

104

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The glpK genes of Enterococcus casseliflavus and Enterococcus faecalis, encoding glycerol kinase, the key enzyme of glycerol uptake and metabolism in bacteria, have been cloned and sequenced. The translated amino acid sequences exhibit strong homology to the amino acid sequences of other bacterial glycerol kinases. After expression of the enterococcal glpK genes in Escherichia coli, both glycerol kinases were purified and were found to be phosphorylated by enzyme I and the histidine-containing protein of the phosphoenolpyruvate: glycose phosphotransferase system. Phosphoenolpyruvate-dependent phosphorylation caused a 9-fold increase in enzyme activity. The site of phosphorylation in glycerol kinase of E. casseliflavus was determined as His-232. Site-specific mutagenesis was used to replace His-232 in glycerol kinase of E. casseliflavus with an alanyl, glutamate, or arginyl residue. The mutant proteins could no longer be phosphorylated confirming that His-232 of E. casseliflavus glycerol kinase represents the site of phosphorylation. The His 232 3 Arg glycerol kinase exhibited an about 3-fold elevated activity compared with wild-type glycerol kinase. Fructose 1,6-bisphosphate was found to inhibit E. casseliflavus glycerol kinase activity. However, neither EIIA Glc from E. coli nor the EIIA Glc domain of Bacillus subtilis had an inhibitory effect on glycerol kinase of E. casseliflavus.Glycerol uptake in Gram-negative and Gram-positive bacteria is mediated by the glycerol diffusion facilitator, an integral membrane protein of 30 kDa, catalyzing the rapid equilibration of concentration gradients of glycerol across the cytoplasmic membrane (1, 2). Intracellular glycerol is converted to glycerol-3-P by the enzyme glycerol kinase that uses ATP as phosphoryl donor (3, 4). Glycerol-3-P is not a substrate of the glycerol diffusion facilitator (5) and hence remains entrapped in the cell, where it is further metabolized. Phosphorylation of glycerol by glycerol kinase provides the driving force for the uptake of glycerol, as it creates a constant imbalance of the glycerol concentrations inside and outside the cell. It was therefore not surprising that glycerol kinase is the target of several regulation mechanisms.

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“…The differences in glycerol utilization between the Δ ptsHI and the strains lacking crr is due to the inhibition of glycerol uptake by unphosphorylated EIIA Glc in S . Typhimurium, as demonstrated by van der Vlag et al ., 1995 [48].…”

Section: Discussionmentioning

confidence: 99%

Nutritional and Metabolic Requirements for the Infection of HeLa Cells by Salmonella enterica Serovar Typhimurium

Bowden

Hopper-Chidlaw

Rice³

et al. 2014

PLoS ONE

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Salmonella is the causative agent of a spectrum of human and animal diseases ranging from gastroenteritis to typhoid fever. It is a food - and water - borne pathogen and infects via ingestion followed by invasion of intestinal epithelial cells and phagocytic cells. In this study we employed a mutational approach to define the nutrients and metabolic pathways required by Salmonella enterica serovar Typhimurium during infection of a human epithelial cell line (HeLa). We deleted the key glycolytic genes, pfkA and pfkB to show that S. Typhimurium utilizes glycolysis for replication within HeLa cells; however, glycolysis was not absolutely essential for intracellular replication. Using S. Typhimurium strains deleted for genes encoding components of the phosphotransferase system and glucose transport, we show that glucose is a major substrate required for the intracellular replication of S. Typhimurium in HeLa cells. We also deleted genes encoding enzymes involved in the utilization of gluconeogenic substrates and the glyoxylate shunt and show that neither of these pathways were required for intracellular replication of S. Typhimurium within HeLa cells.

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Regulation of glycerol and maltose uptake by the IIAGlc-like domain of IINag of the phosphotransferase system inSalmonella typhimurium LT2

Cited by 13 publications

References 30 publications

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Cloning and Sequencing of two Enterococcal glpK Genes and Regulation of the Encoded Glycerol Kinases by Phosphoenolpyruvate-dependent, Phosphotransferase System-catalyzed Phosphorylation of a Single Histidyl Residue

Nutritional and Metabolic Requirements for the Infection of HeLa Cells by Salmonella enterica Serovar Typhimurium

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