Molecular analysis of the mannitol operon of Clostridium acetobutylicum encoding a phosphotransferase system and a putative PTS-modulated regulator

Behrens, Susanne; Mitchell, Wilfrid J.; Bahl, Hubert

doi:10.1099/00221287-147-1-75

Cited by 33 publications

(37 citation statements)

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“…In most DeoR-type transcription activators, a traditional helix-turn-helix motif is located at the beginning of the Nterminal domain. However, in a few PTS-controlled regulators, the helix-turn-helix motif is degenerated and difficult to detect (51). The suggested presence of a second helix-turn-helix motif in LicR (879) has so far not been confirmed.…”

Section: Regulation Of Transcription Activators By Pts-mediated Phospmentioning

confidence: 99%

“…Surprisingly, only a polar insertion into mtlR was reported to prevent mannitol utilization by S. mutans, whereas a nonpolar insertion had no effect (342). Therefore, (51). The DNA binding site for LicR, the second PRD-containing DeoR-type transcription activator in B. subtilis, was determined by carrying out a deletion analysis with the promoter region of the lic operon.…”

Section: Mtlmentioning

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

1,203

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 Transcription Activators By Pts-mediated Phospmentioning

confidence: 99%

Section: Mtlmentioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,203

769

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“…The mixture was equilibrated at 37°C for 3 min, and then [D-glucose 1-14 C] lactose (9.67 mM, 1.03 Ci/mol) was added to a concentration of 0.2 mM. Samples (150 l) of reaction mixture were removed at intervals, and the amount of sugar phosphate formed was estimated as described previously (5).…”

Section: Methodsmentioning

confidence: 99%

Analysis of the Mechanism and Regulation of Lactose Transport and Metabolism in Clostridium acetobutylicum ATCC 824

Tangney

Aass

et al. 2007

Appl Environ Microbiol

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Although the acetone-butanol-ethanol fermentation of Clostridium acetobutylicum is currently uneconomic, the ability of the bacterium to metabolize a wide range of carbohydrates offers the potential for revival based on the use of cheap, low-grade substrates. We have investigated the uptake and metabolism of lactose, the major sugar in industrial whey waste, by C. acetobutylicum ATCC 824. Lactose is taken up via a phosphoenolpyruvate-dependent phosphotransferase system (PTS) comprising both soluble and membrane-associated components, and the resulting phosphorylated derivative is hydrolyzed by a phospho-␤-galactosidase. These activities are induced during growth on lactose but are absent in glucose-grown cells. Analysis of the C. acetobutylicum genome sequence identified a gene system, lacRFEG, encoding a transcriptional regulator of the DeoR family, IIA and IICB components of a lactose PTS, and phospho-␤-galactosidase. During growth in medium containing both glucose and lactose, C. acetobutylicum exhibited a classical diauxic growth, and the lac operon was not expressed until glucose was exhausted from the medium. The presence upstream of lacR of a potential catabolite responsive element (cre) encompassing the transcriptional start site is indicative of the mechanism of carbon catabolite repression characteristic of low-GC gram-positive bacteria. A pathway for the uptake and metabolism of lactose by this industrially important organism is proposed.The acetone-butanol-ethanol (ABE) fermentation of Clostridium acetobutylicum was a classical method to produce the commercially important solvents acetone and butanol, which operated successfully at an industrial scale in many countries during the first half of the 20th century. After the Second World War, the fermentation process declined because of the emergence of the competitive petrochemical-based synthesis of the solvents (18). Nevertheless, oil is a finite commodity and global oil prices are on the rise, and this, coupled with a general worldwide interest in exploiting renewable resources, has stimulated research on the biochemistry and physiology of solventogenic clostridia in recent years, with the aim of exploring the potential for revival of the ABE fermentation (17, 22). A major consideration in any bioconversion process is the availability of a cost-effective and high-product-yielding growth medium, whereby there is maximal conversion of the available carbon into the commercial end product. The substrate of choice in the traditional industrial ABE fermentation, molasses, accounted for more than 60% of the overall cost of the process (19). However, the clostridia are metabolically versatile with respect to carbohydrate utilization and the potential therefore exists to exploit alternative, cheaper, low-grade substrates.Several clostridial strains are able to produce solvents by fermentation of whey (21), which has been shown to be economically superior to the traditional process (19). Despite low reactor productivity, an attractive feature of these fermenta...

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“…In contrast, mannitol metabolism has been intensively studied in Escherichia coli (19) and other bacteria, such as Bacillus subtilis (20,21), Bacillus stearothermophilus (22), Clostridium acetobutylicum (23), and Streptococcus mutans (24). In these terrestrial bacteria, mannitol is taken up by a mannitol-specific phosphoenolpyruvate/carbohydrate phosphotransferase system (PTS) and is phosphorylated into M1P during its transport, and M1P is further oxidized to F6P by a M1P-specific dehydrogenase (25) before entering glycolysis.…”

mentioning

confidence: 99%

“…In the soil bacterium Acinetobacter baylyi (26), the M1P dehydrogenase is fused to a haloacid dehalogenase (HAD)-like phosphatase domain at the N terminus that was shown to catalyze M1Pase activity (27). In C. acetobutylicum (23) and B. stearothermophilus (22), the mannitol catabolic operon is regulated by two mechanisms: a glucose-mediated catabolite repression and a transcriptional activation mechanism controlled by MtlR using mannitol as an inducer. Other bacteria, such as Pseudomonas fluorescens, are known to contain a mannitol-2-dehydrogenase, an enzyme that oxidizes mannitol into fructose; mannitol is transported by ATP binding cassette (ABC) transporters (28).…”

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confidence: 99%

The Mannitol Utilization System of the Marine Bacterium Zobellia galactanivorans

Groisillier

Labourel

Michel

et al. 2015

Appl Environ Microbiol

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Mannitol is a polyol that occurs in a wide range of living organisms, where it fulfills different physiological roles. In particular, mannitol can account for as much as 20 to 30% of the dry weight of brown algae and is likely to be an important source of carbon for marine heterotrophic bacteria. Zobellia galactanivorans (Flavobacteriia) is a model for the study of pathways involved in the degradation of seaweed carbohydrates. Annotation of its genome revealed the presence of genes potentially involved in mannitol catabolism, and we describe here the biochemical characterization of a recombinant mannitol-2-dehydrogenase (M2DH) and a fructokinase (FK). Among the observations, the M2DH of Z. galactanivorans was active as a monomer, did not require metal ions for catalysis, and featured a narrow substrate specificity. The FK characterized was active on fructose and mannose in the presence of a monocation, preferentially K ؉ . Furthermore, the genes coding for these two proteins were adjacent in the genome and were located directly downstream of three loci likely to encode an ATP binding cassette (ABC) transporter complex, suggesting organization into an operon. Gene expression analysis supported this hypothesis and showed the induction of these five genes after culture of Z. galactanivorans in the presence of mannitol as the sole source of carbon. This operon for mannitol catabolism was identified in only 6 genomes of Flavobacteriaceae among the 76 publicly available at the time of the analysis. It is not conserved in all Bacteroidetes; some species contain a predicted mannitol permease instead of a putative ABC transporter complex upstream of M2DH and FK ortholog genes. Brown algae (Phaeophyceae) are the dominant macroalgae in temperate and polar regions and thus play a crucial role in the primary production of coastal ecosystems (1). They contain large amounts of different structural and storage carbohydrates. For instance, their extracellular matrices are formed by the accumulation of cellulose, fucanes, and alginates (2-4), while they store carbon by accumulating laminarin and mannitol (5). The potential of this biomass resource for the production of liquid biofuels (6), including ethanol from alginate and mannitol (7,8), and for the implementation of biorefineries (9) has been highlighted recently.Depending on the species, mannitol can represent as much as 20 to 30% of the dry weight of brown seaweed (10). In the genomic and genetic model of brown algae Ectocarpus sp., formerly included in the species Ectocarpus siliculosus (11), it has been observed that the content of this polyol differs according to the diurnal cycle (12) and that it is likely to act as an osmoprotectant or a local compatible osmolyte (13). Mannitol is localized in the cytosol and is also present at the reducing ends of vacuolar laminarin molecules of the M series (in contrast to the G series, which contain only glucose residues) (14). Mannitol in brown algae is produced directly from the photoassimilate fructose-6-phosphate (F6P) by two st...

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Molecular analysis of the mannitol operon of Clostridium acetobutylicum encoding a phosphotransferase system and a putative PTS-modulated regulator

Abstract: Clostridium acetobutylicum DSM 792 accumulates and phosphorylates mannitol via a phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS).

Cited by 33 publications

References 59 publications

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

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

Analysis of the Mechanism and Regulation of Lactose Transport and Metabolism in Clostridium acetobutylicum ATCC 824

The Mannitol Utilization System of the Marine Bacterium Zobellia galactanivorans

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