Isolation of a novel protein involved in the transport of fructose by an inducible phosphoenolpyruvate fructose phosphotransferase system in Streptococcus mutans

Gauthier, Lucie; Mayrand, D.; Vadeboncoeur, Christian

doi:10.1128/jb.160.2.755-763.1984

Cited by 35 publications

(32 citation statements)

References 50 publications

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“…The presence of this constitutive Eir™ in S. mutans was confirmed by the isolation of EIF^-negative mutants that still possessed glucose and mannose PTS activities (38). These EIF™-negative mutants are, however, able to grow ot\ fructose owing to the presence of another inducible EII'™ that functions with an inducible IIF™ (8).…”

Section: Discussionmentioning

confidence: 90%

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

Néron

Vadeboncoeur

1987

Oral Microbiology and Immunology

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Spontaneous phosphotransferase negative mutants of Streptococcus mutans GS5‐2 (mutant GM500) and of Streptococcus sobrinus 27352 (mutant MM202) were isolated by screening for 2‐deoxyglucose resistance using lactose as the growth substrate. Measurements of phosphoenolpyruvate: phosphotransferase activities with isolated membranes and purified Enzyme I and HPr indicated that the mutant strains were defective at the level of membrane components of the phosphoenolpyruvate: mannose phosphotranferase system but still possessed phosphoenolpyruvate: glucose phosphotransferase activity. These results were corroborated by uptake studies performed with resting cells. Our results suggest that glucose is transported by 2 distinct phosphoenolpyruvate: phosphotransferase systems in S. mutans and S. sobrinus, one of which is also capable of transporting mannose. This glucose‐mannose transport system is involved in catabolite repression and inducer exclusion, and controls, by way of these mechanisms, the metabolism of lactose.

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Section: Discussionmentioning

confidence: 90%

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

Néron

Vadeboncoeur

1987

Oral Microbiology and Immunology

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“…Their X"cells (like ours) metabolized fructose normally after xylitol exposure, no futile cycle taking place during the incubation with the pentitol. Fructose metabolism by glucose grown X"^ strains (Ell;, fructose PTS negative) is possible since the inducible EII fructose and the Elllf^u component of the PTS are induced during growth of S. mutans in glucose-supplemented TYE mediutn (11). Moreover, it is also known that the EII rnannose PTS from another oral streptococcus {S. salivarius) phosphorylates fructose (41); it could also happen in S. sobrinus.…”

Section: Effects Of Tiie Xyiitoi Uptake And/or Tiie Intraceiiuiar Xyimentioning

confidence: 99%

“…In this study xyhtol was not significantly transported by the inducible fructose PTS in the X" mutant (constitutive fructose PTS negative) grown on fructose. Such a difference of affinity between the constitutive and the inducible Ellf^u might be explained by the fact that the constitutive Ellf^u of S. mutans phosphorylates fructose on carbon 6, whereas the inducible EII phosphorylates this hexose on carbon 1 (11). The 5 carbon xylitol being a symmetrical molecule, carbons 1 and 2 and 4 and 5 are equivalent and have the same configuration as carbons 5 and 6 of fructose.…”

Section: Xyiitoi Uptake and Efflux Mechanismmentioning

confidence: 99%

Intracellular xylitol‐phosphate hydrolysis and efflux of xylitol in Streptococcus sobrinus

Trahan

Néron

Bareil

1991

Oral Microbiology and Immunology

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The parental strain Streptococcus sobrinus (Streptococcus mutans ATCC 27352), which is known to transport, phosphorylate and accumulate xylitol intracellularly as nonmetabolizable xylitol-phosphate (xylitol-sensitive (XS) strain) and its xylitol-resistant (XR) spontaneous mutant were used to further investigate the inhibitory action of xylitol on oral streptococci. Fructose-grown XR cells did not accumulate xylitol-phosphate, indicating that the inducible fructose PTS is incapable of transporting the pentitol. The intracellularly accumulated pentitol-phosphate by the XS cells did not prevent the subsequent uptake and degradation of glucose or fructose, despite a drop in the PEP pool and a 50% inhibition of the glucose but not the fructose catabolism. Intracellular dephosphorylation of the pentitol-phosphate and release of xylitol in the extracellular medium resulted in a rapid decrease of the intracellular level of this nonmetabolizable product. A Mg(++)- or Mn(++)-independent sugar-phosphate hydrolysing activity capable of splitting xylitol-phosphate was demonstrated in both XS and XR strains. Preincubation in the presence of N1-ethylmaleimide (NEM) and xylitol or NEM and fructose resulted in the subsequent inhibition of both xylitol uptake and efflux. The efflux kinetic at various temperatures is compatible with a facilitated diffusion by the phosphotransferase system EIIfru without, however, excluding the existence of an additional exit route, but it excludes a simple diffusion exit process. The results are consistent with the existence of a xylitol futile cycle contributing to the growth inhibition of S. sobrinus by the pentitol without excluding a toxic effect of xylitol-phosphate. Discrepancies in the literature on the action of xylitol on S. mutans could be explained in the light of the evidence presented.

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“…Using spontaneous mutants, Bourassa and Vadeboncoeur [5] biochemically characterized a 57.5-kDa fructose permease in S. salivarius. Gauthier et al [6] isolated a 12-kDa domain A of an inducible fructose^PTS and also provided indirect evidence for the presence of two fructose^PTSs in S. mutans, one inducible and one constitutive [7]. However, little information is available about molecular aspects of fructose utilization by oral streptococci.…”

Section: Introductionmentioning

confidence: 99%

Characterization of two operons that encode components of fructose-specific enzyme II of the sugar:phosphotransferase system of Streptococcus mutans

Wen

Browngardt

Burne

2001

FEMS Microbiology Letters

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Three genes, designated as fruC, fruD and fruI, were predicted to encode polypeptides homologous to fructose-specific enzyme II (II(Fru)) of the phosphoenolpyruvate-dependent sugar:phosphotransferase system, and were cloned from Streptococcus mutans, the primary etiological agent of human dental caries. The fruC and fruD genes encoded domains BC and domain A of II(Fru), respectively. The fruI gene encoded IICBA(Fru). Northern hybridization and slot blot analysis showed that expression of fruI was inducible by sucrose and fructose, while fruCD were expressed constitutively and at much lower levels. Inactivation of either fruI or fruCD alone, or of both fruCD and fruI, had no major impact on growth on fructose at a concentration of 0.5% (w/v). However, when the strains were grown with 0.2% fructose as the sole carbohydrate source, a significant decrease in the growth rate was seen with the fruCD/fruI double mutants. Assays of sugar:phosphotransferase activity showed that the fruCD/fruI double mutants had roughly 30% of the capacity of the wild-type strain to transport fructose via the phosphoenolpyruvate-dependent sugar:phosphotransferase system. Xylitol toxicity assays indicated that the inducible fructose permease was responsible for xylitol transport.

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Isolation of a novel protein involved in the transport of fructose by an inducible phosphoenolpyruvate fructose phosphotransferase system in Streptococcus mutans

Cited by 35 publications

References 50 publications

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

Two functionally different glucose phosphotransferase transport systems in Streptococcus mutans and Streptococcus sobrinus

Intracellular xylitol‐phosphate hydrolysis and efflux of xylitol in Streptococcus sobrinus

Characterization of two operons that encode components of fructose-specific enzyme II of the sugar:phosphotransferase system of Streptococcus mutans

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