Transport of glucose and mannose by a common phosphoenolpyruvate-dependent phosphotransferase system in Streptococcus mutans GS5

Liberman, E S; Bleiweis, Arnold S.

doi:10.1128/iai.43.3.1106-1109.1984

Cited by 40 publications

(18 citation statements)

References 12 publications

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“…Moreover, whole cells of the mutant strains were able to accumulate glucose under conditions that inhibit active transport mechanisms other than the PTS, but were defective in their ability to accumulate 2DG, a mannose analogue. Since it has already been shown that EII""'" can also phosphorylate glucose (13,39), results presented in this paper indicated that S. mutans and S. sobrinus possess two distinct PTS that could phosphorylate glucose as we have already suggested in the past (39). It thus appears that lactic and oral streptococci have different PTS structures.…”

Section: Discussionsupporting

confidence: 64%

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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: Discussionsupporting

confidence: 64%

“…The carbohydrates glucose, fructose and mannose are PTS sugars in Grampositive streptococci (13,30,31,33,39). However, information concerning the number and the nature of the specific components involved in the transport of these sugars is scarce, and sometimes conflicting.…”

Section: Discussionmentioning

confidence: 99%

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

Néron

Vadeboncoeur

1987

Oral Microbiology and Immunology

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“…These results strongly suggest that the abovedescribed activities are all due to a single constitutive PTS, i.e., Man-PTS, a nomenclature after the similar constitutive PTS of enterobacteria (10). Man-PTS with a similar substrate specificity has also been described for other lactic acid bacteria (2,6,8,9,17). Strain LAC 12 showed no PTS activity for methyl-a-D-glucoside, indicating that the strain has no "Glc-PTS" known in enterobacteria (10).…”

mentioning

confidence: 55%

Existence of Phosphoenolpyruvate: Carbohydrate Phosphotransferase Systems in Lactobacillus fermentum, an Obligate Heterofermenter

Nagasaki

Ito

Matsuzaki

et al. 1992

Microbiology and Immunology

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The presence or absence of the phosphoenolpyruvate : carbohydrate phosphotransferase system (PTS) in obligately heterofermentative group III lactobacilli including Lactobacillus brevis (3 strains), L. buchneri (2 strains) and L. fermentum (3 strains) was surveyed systematically for a series of sugars utilizable by these organisms. Contrary to common expectation, PTSs were found in two strains of L. fermentum: sucrose-PTS in one strain; sucrose-and mannose-PTSs in the other. All these activities were found to be constitutive.The phosphoenolpyruvate (PEP) : carbohydrate phosphotransferase system (PTS) is a unique sugar transport system found in bacteria. This system catalyzes the transport and concomitant phosphorylation of a number of sugars. A PTS generally consists of four proteins : enzyme I and HPr (heat-stable protein) common to all PTSs, and enzymes II and III specific for a sugar. The distribution of PTS is not ubiquitous, and when it exists, the range of sugars transported by PTS varies greatly with the bacterial species (11).Romano et al (13) studied the distribution of PTS among lactic acid bacteria by examining PTS activity for 2-deoxy-D-glucose (2DG), a non-metabolizable analogue of glucose (Glc) or mannose (Man). The PTS was present in the homofermenters such as streptococci, pediococci, and group II lactobacilli including Lactobacillus casei and L. plantarum that metabolize Glc via the Embden-MeyerhofParnas (EMP) pathway, but was absent in the heterofermenters such as leuconostocs, group III lactobacilli including L. brevis and L. buchneri, and bifidobacteria that metabolize Glc via non-EMP pathways. Since then, it is believed that PTS is linked to the EMP mode of glycolysis, that is, when a sugar is transported by a PTS, the sugar is metabolized via the EMP pathway (11). Recently, Reizer et al (12) found that certain L. brevis and L. buchneri strains had a protein similar to HPr, but no enzyme I, and concluded that a complete PTS could not operate in these organisms.We report here on a more comprehensive survey of PTSs in strains of group III lactobacilli including L. brevis, L. buchneri and L. fermentum. Unexpectedly, functional

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“…In streptococcal cells only the presence of the mannose/glucose/2-deoxyglucose permease has been established [26,27]. There are conflicting reports about the presence of an additional glucose/a-methylglucoside transport system in oral streptococci [28,29]. Similarly,, III gl~, involved in the uptake of glucose/a-methylglucoside in Gram-negative bacteria, has not been detected in Gram-positive bacteria.…”

Section: Discussionmentioning

confidence: 99%

Phosphoenolpyruvate-dependent phosphorylation of a 55-kDa protein of Streptococcus faecalis catalyzed by the phosphotransferase system

Deutscher

1985

FEMS Microbiology Letters

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A protein with an Mr of 55000 was isolated from glucose‐grown Streptococcus faecalis cells. The protein becomes phosphorylated in a phosphoenolpyruvate‐dependent reaction catalyzed by enzyme I and HPr of the bacterial phosphotransferase system. It did not stimulate phosphoenolpyruvate‐dependent glucose phosphorylation. Several sugars were tested for their ability to dephosphorylate the phosphorylated protein in the presence of membrane fragments. Even though some of the sugars were able to dephosphorylate phospho‐HPr quickly, the factor III‐like 55‐kDa protein remained phosphorylated. We therefore assumed that this protein is not involved in any sugar uptake reaction but that it exerts a regulatory function in Gram‐positive bacteria comparable to the function of factor III specific for glucose in Escherichia coli.

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Transport of glucose and mannose by a common phosphoenolpyruvate-dependent phosphotransferase system in Streptococcus mutans GS5

Cited by 40 publications

References 12 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

Existence of Phosphoenolpyruvate: Carbohydrate Phosphotransferase Systems in Lactobacillus fermentum, an Obligate Heterofermenter

Phosphoenolpyruvate-dependent phosphorylation of a 55-kDa protein of Streptococcus faecalis catalyzed by the phosphotransferase system

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