Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol

Wehtje, Christina; Beijer, Lena; Nilsson, Rune‐Pär; Rutberg, Blanka

doi:10.1099/13500872-141-5-1193

Cited by 18 publications

(18 citation statements)

References 35 publications

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“…The site of PEP-dependent, EI-and HPr-catalyzed phosphorylation was determined to be His-232 in GlpK of E. casseliflavus (109) and His-230 in GlpK of B. subtilis (158). Interestingly, in one of the B. subtilis suppressor mutants that were able to grow on glycerol despite the absence of active EI and HPr, His-230 of GlpK was replaced with an arginine, and in another mutant, the neighboring Phe-232 was replaced with a serine (937). These mutations were thought to cause structural changes similar to those triggered by phosphorylation, and the ability of these glpK mutants to grow on glycerol was assumed to be due to PTS-independent elevated activity of the mutant GlpKs.…”

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

confidence: 99%

“…Nevertheless, suppressor mutants that restored growth of a B. subtilis ptsHI mutant on glycerol have been obtained (52). They were not affected in ptsG but, rather, were affected in glpK (937), and glycerol uptake in gram-positive bacteria was therefore assumed to be regulated by an EIIA Glc -independent mechanism.…”

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

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,204

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%

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

1,204

769

View full text Add to dashboard Cite

show abstract

“…PTS-mediated GlpK stimulation therefore follows a longrange activation mechanism. Studies with an E. faecalis GlpK mutant protein in which the regulatory His-232 had been replaced with an arginine, which leads to a fully active enzyme without phosphorylation (46), suggested that phosphorylation induces structural rearrangements along the dimer interface that allow an optimal positioning of a crucial arginine residue (Arg-18) in the active site (47).…”

Section: Proteins Containing Their Own Pts-recognized Phosphorylationmentioning

confidence: 99%

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Deutscher

Aké

Derkaoui

et al. 2014

Microbiol Mol Biol Rev

354

374

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SUMMARY The bacterial phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) carries out both catalytic and regulatory functions. It catalyzes the transport and phosphorylation of a variety of sugars and sugar derivatives but also carries out numerous regulatory functions related to carbon, nitrogen, and phosphate metabolism, to chemotaxis, to potassium transport, and to the virulence of certain pathogens. For these different regulatory processes, the signal is provided by the phosphorylation state of the PTS components, which varies according to the availability of PTS substrates and the metabolic state of the cell. PEP acts as phosphoryl donor for enzyme I (EI), which, together with HPr and one of several EIIA and EIIB pairs, forms a phosphorylation cascade which allows phosphorylation of the cognate carbohydrate bound to the membrane-spanning EIIC. HPr of firmicutes and numerous proteobacteria is also phosphorylated in an ATP-dependent reaction catalyzed by the bifunctional HPr kinase/phosphorylase. PTS-mediated regulatory mechanisms are based either on direct phosphorylation of the target protein or on phosphorylation-dependent interactions. For regulation by PTS-mediated phosphorylation, the target proteins either acquired a PTS domain by fusing it to their N or C termini or integrated a specific, conserved PTS regulation domain (PRD) or, alternatively, developed their own specific sites for PTS-mediated phosphorylation. Protein-protein interactions can occur with either phosphorylated or unphosphorylated PTS components and can either stimulate or inhibit the function of the target proteins. This large variety of signal transduction mechanisms allows the PTS to regulate numerous proteins and to form a vast regulatory network responding to the phosphorylation state of various PTS components.

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“…Mutations that bypass this dependency were isolated and found to be in glpK, the gene encoding glycerol kinase which generates glycerol 3-phosphate, the internal inducer of the glp regulon in B. subtilis (Wehtje et al, 1995). Subsequently, direct phosphorylation of glycerol kinase by EI and HPr was demonstrated (Charrier et al, 1997).…”

Section: Pts-associated Proteinsmentioning

confidence: 99%

Novel phosphotransferase system genes revealed by genome analysis – the complete complement of PTS proteins encoded within the genome of Bacillus subtilis

et al. 1999

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Bacillus subtilis can utilize several sugars as single sources of carbon and energy. Many of these sugars are transported and concomitantly phosphorylated by the phosphoenolpyruvate :sugar phosphotransferase system (PTS). In addition to its role in sugar uptake, the PTS is one of the major signal transduction systems in B. subtilis. In this study, an analysis of the complete set of PTS proteins encoded within the B. subtilis genome is presented. Fifteen sugar-specific PTS permeases were found to be present and the functions of novel PTS permeases were studied based on homology to previously characterized permeases, analysis of the structure of the gene clusters in which the permease encoding genes are located and biochemical analysis of relevant mutants. Members of the glucose, sucrose, lactose, mannose and fructose/mannitol families of PTS permeases were identified. Interestingly, nine pairs of IIB and IIC domains belonging to the glucose and sucrose permease families are present in B. subtilis ; by contrast only five Enzyme IIA Glc -like proteins or domains are encoded within the B. subtilis genome. Consequently, some of the EIIA Glc -like proteins must function in phosphoryl transfer to more than one IIB domain of the glucose and sucrose families. In addition, 13 PTS-associated proteins are encoded within the B. subtilis genome. These proteins include metabolic enzymes, a bifunctional protein kinase/phosphatase, a transcriptional cofactor and transcriptional regulators that are involved in PTS-dependent signal transduction. The PTS proteins and the auxiliary PTS proteins represent a highly integrated network that catalyses and simultaneously modulates carbohydrate utilization in this bacterium.

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Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol

Cited by 18 publications

References 35 publications

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

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

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Novel phosphotransferase system genes revealed by genome analysis – the complete complement of PTS proteins encoded within the genome of Bacillus subtilis

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