Pel, the protein that permits lambda DNA penetration of Escherichia coli, is encoded by a gene in ptsM and is required for mannose utilization by the phosphotransferase system.

Williams, Noreen; Fox, Donna K.; Shea, Catherine; Roseman, Saul

doi:10.1073/pnas.83.23.8934

Cited by 47 publications

(59 citation statements)

References 24 publications

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“…It was therefore proposed that the membrane components of the mannose/glucose PTS are necessary for the docking of the bacteriocin. Interestingly, the E. coli membranespanning mannose-specific PTS components are also important for the infection by bacteriophage lambda (218,950), and they can be replaced in lambda infection by the B. subtilis PTS components of the lev operon (525).…”

Section: Discussionmentioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,162

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: Discussionmentioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,162

769

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“…However, either the same protein or a similar one is also present that phosphorylates 2-deoxyglucose and, in some cases, perhaps fructose. If a single sugar-specific membrane protein catalyzes these sugar phosphorylations and interacts with phospho-IIIGIc, this would suggest a possible evolutionary origin of the enteric bacterial genes that specify II-BGIc and the three genes of the ptsM region (47). That is, they may have arisen from a common precursor gene that has been conserved in some of the vibrios.…”

Section: Discussionmentioning

confidence: 99%

“…Chem., in press) and is critical for many of the regulatory phenomena summarized above. The 1IMan system is the only one yet described in which the sugar-specific membrane enzyme complex consists of three proteins (47). The IIG1c and IIMan systems are assayed with the analogs-methyl a-glucoside and 2-deoxyglucose, respectively (42).…”

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confidence: 99%

Phosphoenolpyruvate:glycose phosphotransferase system in species of Vibrio, a widely distributed marine bacterial genus

et al. 1987

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The genus Vibrio is one of the most common and widely distributed groups of marine bacteria. Studies on the physiology of marine Vibrio species were initiated by examining 15 species for the bacterial phosphoenolpyruvate:glycose phosphotransferase system (PTS). All species tested contained a PTS analogous to the glucose-specific (IIGIc) system in enteric bacteria. Crude extracts of the cells showed immunological cross-reactivity with antibodies to enzyme I, HPr, and IIIGIc from Salmonella typhimurium when assayed by the rocket-line method. Toluene-permeabilized cells of 11 species were tested and were active in phosphorylating methyl a-D-glucoside with phosphoenolpyruvate but not ATP as the phosphoryl donor. Membranes from 10 species were assayed, and they phosphorylated methyl a-D-glucoside when supplemented with a phosphoHIGIc.generating system composed of homogeneous proteids from enteric bacteria. Toluene-permeabilized cells and membranes of seven species were assayed, as were phosphorylated fructose and 2-deoxyglucose. 111GIc was isolated from Vibriofluvialis and was active in phosphorylating methyl a-D-glucoside when supplemented with a phospho-HPr-generating system composed of homogeneous proteins from Escherichia coli and membranes from either E. coli or V. fluvialis. These results show that the bacterial PTS is widely distributed in the marine environment and that it is likely to have a significant role in marine bacterial physiology and in the marine ecosystem.The phosphoenolpyruvate:glycose phosphotransferase system (PTS) is a complex system of interacting cytoplasmic and membrane proteins with diverse functions in the bacterial cell (for recent reviews, see references 29 and 36). For example, the PTS concomitantly phosphorylates and translocates its sugar substrates across the cytoplasmic membrane, is involved in chemotaxis toward these sugars, regulates the uptake of at least some lion-PTS sugars, regulates adenylate cyclase, and controls the transcription of operons required for the utilization of non-PTS sugars. Through these regulatory functions, the PTS is largely responsible for the phenomenon called diauxic growth in enteric bacteria.

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“…The ptsM locus has been renamed (11), and contains the genes manX, manY, and manZ. The relevant manXYZ genotype, if known, is given.…”

Section: Phenotypes Of E Coli Transformants Carrying Glcmentioning

confidence: 99%

Sugar Transport by the Marine Chitinolytic Bacterium Vibrio furnissii

Bouma

Roseman

1996

Journal of Biological Chemistry

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Chitin catabolism by the marine bacterium Vibrio furnissii involves chemotaxis to and transport of N-acetyl-D-glucosamine (GlcNAc) and D-glucose. We report the properties of the respective permeases that complemented E. Glc for sugar fermentation in vivo and phosphorylation in vitro. While there are similarities between the phosphoenolpyruvate:glycose phosphotransferase system of V. furnissii and enteric bacteria, the differences may be important for survival of V. furnissii in the marine environment.Chitin, a ␤,134-linked polymer of N-acetylglucosamine (GlcNAc), is one of the most abundant organic compounds in nature. Huge quantities of this highly insoluble polysaccharide are turned over annually in the aquatic biosphere, and marine bacteria such as Vibrios are major biological components of this ecologically indispensable process.In previous papers (1-4), we reported that chitin degradation by one such organism, Vibrio furnissii, is extraordinarily complex, involving multiple signal transduction systems and many proteins. We proposed (4) that the means by which these cells locate chitin-containing organisms is by chemotaxis to components of the hemolymph and molt fluids including glucose, trehalose, GlcNAc and chitin oligosaccharides; all of these compounds are potent chemoattractants for V. furnissii.Degradation of chitin by V. furnissii is initiated by chitinases that hydrolyze it to soluble oligosaccharides, which are further hydrolyzed in the periplasmic space to GlcNAc and (GlcNAc) 2 . Finally, each of these catabolites is taken up by specific transporters and converted intracellularly to Fru-6-P, NH 3 , and acetate. The cytoplasmic membrane permeases are, therefore, essential components of the chitin catabolic cascade. The disaccharide permease is described in an accompanying paper (5), while the present report is concerned with the GlcNAc and Glc chemoreceptors/permeases.We have presented evidence that the uptake and phosphorylation of GlcNAc, Glc, and Man in V. furnissii is mediated by the bacterial phosphoenolpyruvate:glycose phosphotransferase system (PTS).1 While the complete PTS is required for both chemotaxis and transport, the sugar chemoreceptors/translocators are the membrane-associated Enzyme II complexes (for reviews see Refs. 6 and 7).2 The Enzyme II complexes often show overlapping substrate specificities. For example, in Escherichia coli and Salmonella typhimurium, GlcNAc is recognized and taken up by II Nag , and Glc by the protein pair II Glc /III Glc , but both substrates are also taken up by the less specific, more complex mannose system, II Man . For this reason, definitive characterization of the specificities of the V. furnissii Enzyme II complexes requires that they be separated from one another.In this and accompanying papers (8, 9), we describe the molecular cloning and characterization of genes and gene products from V. furnissii into E. coli that generate GlcNAc in the periplasmic space, and recognize and transport GlcNAc, Glc, and Man. The V. furnissii proteins are physiologi...

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Pel, the protein that permits lambda DNA penetration of Escherichia coli, is encoded by a gene in ptsM and is required for mannose utilization by the phosphotransferase system.

Cited by 47 publications

References 24 publications

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

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

Phosphoenolpyruvate:glycose phosphotransferase system in species of Vibrio, a widely distributed marine bacterial genus

Sugar Transport by the Marine Chitinolytic Bacterium Vibrio furnissii

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