The
            <i>Bacillus subtilis</i>
            AraE Protein Displays a Broad Substrate Specificity for Several Different Sugars

Krispin, Oliver; Allmansberger, Rudolf

doi:10.1128/jb.180.12.3250-3252.1998

Cited by 68 publications

(35 citation statements)

References 14 publications

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“…While possessing all proteins necessary to degrade D-galactose, B. subtilis 168 1A1 is unable to grow in minimal medium with this sugar as the sole carbon source, owing to the lack of a specific transporter. However, D-galactose is imported when L-arabinose is also added to the minimum medium (Krispin & Allmansberger, 1998). Bacillus subtilis 168 1A1 and two isogenic mutants, BFS2613 or BFS2619 (in which yoxA or dacC had been disrupted, respectively), were grown in M9 medium with 5 mM D-galactose as the main carbon source and 1 mM L-arabinose to induce the AraE transporter synthesis.…”

Section: Growth Of B Subtilis 168 1a1 Bfs2613 and Bfs2619 Strains Imentioning

confidence: 99%

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Duez¹,

Zervosen²,

Teller³

et al. 2009

FEMS Microbiology Letters

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In Bacillus subtilis, the yoxA and dacC genes were proposed to form an operon. The yoxA gene was overexpressed in Escherichia coli and its product fused to a polyhistidine tag was purified. An aldose-1-epimerase or mutarotase activity was measured with the YoxA protein that we propose to rename as GalM by analogy with its counterpart in E. coli. The peptide D-Glu-delta-m-A(2)pm-D-Ala-m-A(2)pm-D-Ala mimicking the B. subtilis and E. coli interpeptide bridge was synthesized and incubated with the purified dacC product, the PBP4a. A clear dd-endopeptidase activity was obtained with this penicillin-binding protein, or PBP. The possible role of this class of PBP, present in almost all bacteria, is discussed.

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Section: Growth Of B Subtilis 168 1a1 Bfs2613 and Bfs2619 Strains Imentioning

confidence: 99%

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Duez¹,

Zervosen²,

Teller³

et al. 2009

FEMS Microbiology Letters

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“…Until now, only two mechanisms of D-xylose transport have been characterized in bacteria. One mechanism, identified in Escherichia coli (5,6), Salmonella typhimurium (29), Bacillus megaterium (28), Lactobacillus brevis (1), Bacillus subtilis (12,27), Tetragenococcus halophila (35), and some ruminal bacteria (31,33), involves a D-xylose-H ϩ or -Na ϩ symporter. The second mechanism consists of a high-affinity D-xylose transport system involving a periplasmic binding protein and is driven by ATP.…”

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confidence: 99%

Transport of d-Xylose in Lactobacillus pentosus, Lactobacillus casei, andLactobacillus plantarum: Evidence for a Mechanism of Facilitated Diffusion via the Phosphoenolpyruvate:Mannose Phosphotransferase System

1999

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We have identified and characterized the d-xylose transport system of Lactobacillus pentosus. Uptake ofd-xylose was not driven by the proton motive force generated by malolactic fermentation and required d-xylose metabolism. The kinetics of d-xylose transport were indicative of a low-affinity facilitated-diffusion system with an apparent Km of 8.5 mM and aV max of 23 nmol min−1 mg of dry weight−1. In two mutants of L. pentosusdefective in the phosphoenolpyruvate:mannose phosphotransferase system, growth on d-xylose was absent due to the lack ofd-xylose transport. However, transport of the pentose was not totally abolished in a third mutant, which could be complemented after expression of the L. curvatus manB gene encoding the cytoplasmic EIIBMan component of the EIIMancomplex. The EIIMan complex is also involved ind-xylose transport in L. casei ATCC 393 andL. plantarum 80. These two species could transport and metabolize d-xylose after transformation with plasmids which expressed the d-xylose-catabolizing genes of L. pentosus, xylAB. L. casei and L. plantarum mutants resistant to 2-deoxy-d-glucose were defective in EIIMan activity and were unable to transportd-xylose when transformed with plasmids containing thexylAB genes. Finally, transport of d-xylose was found to be the rate-limiting step in the growth of L. pentosus and of L. plantarum and L. caseiATCC 393 containing plasmids coding for thed-xylose-catabolic enzymes, since the doubling time of these bacteria on d-xylose was proportional to the level of EIIMan activity.

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“…Decreased intracellular xylose concentration would alter the ratio of unbound to xylose-bound XylR repressor, which would promote XylR-mediated repression of the XylR-controlled gene. Reduction of intracellular xylose concentration could be further exacerbated if the predicted sugar/ cation symporter CA_C1339 (araE1) transports both arabinose and xylose, as has been demonstrated for many bacterial pentose transporters, such as in B. subtilis, E. coli, and Salmonella enterica serovar Typhimurium (42,43). Previous transcriptomic data suggested that CA_C1339 (araE1) was a xylose-specific transporter; however, bioinformatic analysis found an AraR binding site in its promoter region, implying a role in arabinose transport as well (19).…”

Section: Discussionmentioning

confidence: 99%

Arabinose-Induced Catabolite Repression as a Mechanism for Pentose Hierarchy Control in Clostridium acetobutylicum ATCC 824

et al. 2018

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Bacterial fermentation of carbohydrates from sustainable lignocellulosic biomass into commodity chemicals by the anaerobic bacteriumClostridium acetobutylicumis a promising alternative source to fossil fuel-derived chemicals. Recently, it was demonstrated that xylose is not appreciably fermented in the presence of arabinose, revealing a hierarchy of pentose utilization in this organism (L. Aristilde, I. A. Lewis, J. O. Park, and J. D. Rabinowitz, Appl Environ Microbiol 81:1452–1462, 2015,https://doi.org/10.1128/AEM.03199-14). The goal of the current study is to characterize the transcriptional regulation that occurs and perhaps drives this pentose hierarchy. Carbohydrate consumption rates showed that arabinose, like glucose, actively represses xylose utilization in cultures fermenting xylose. Further, arabinose addition to xylose cultures led to increased acetate-to-butyrate ratios, which indicated a transition of pentose catabolism from the pentose phosphate pathway to the phosphoketolase pathway. Transcriptome sequencing (RNA-Seq) confirmed that arabinose addition to cells actively growing on xylose resulted in increased phosphoketolase (CA_C1343) mRNA levels, providing additional evidence that arabinose induces this metabolic switch. A significant overlap in differentially regulated genes after addition of arabinose or glucose suggested a common regulation mechanism. A putative open reading frame (ORF) encoding a potential catabolite repression phosphocarrier histidine protein (Crh) was identified that likely participates in the observed transcriptional regulation. These results substantiate the claim that arabinose is utilized preferentially over xylose inC. acetobutylicumand suggest that arabinose can activate carbon catabolite repression via Crh. Furthermore, they provide valuable insights into potential mechanisms for altering pentose utilization to modulate fermentation products for chemical production.IMPORTANCEClostridium acetobutylicumcan ferment a wide variety of carbohydrates to the commodity chemicals acetone, butanol, and ethanol. Recent advances in genetic engineering have expanded the chemical production repertoire ofC. acetobutylicumusing synthetic biology. Due to its natural properties and genetic engineering potential, this organism is a promising candidate for converting biomass-derived feedstocks containing carbohydrate mixtures to commodity chemicals via natural or engineered pathways. Understanding how this organism regulates its metabolism during growth on carbohydrate mixtures is imperative to enable control of synthetic gene circuits in order to optimize chemical production. The work presented here unveils a novel mechanism via transcriptional regulation by a predicted Crh that controls the hierarchy of carbohydrate utilization and is essential for guiding robust genetic engineering strategies for chemical production.

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The Bacillus subtilis AraE Protein Displays a Broad Substrate Specificity for Several Different Sugars

Abstract: Bacillus subtilis 168 is unable to grow on xylose and galactose as sole carbon sources, owing to the lack of specific transporters. We show that they are imported into the cell by the activity of AraE, an arabinose transporter whose synthesis is induced by l-arabinose.

Cited by 68 publications

References 14 publications

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Transport of d-Xylose in Lactobacillus pentosus, Lactobacillus casei, andLactobacillus plantarum: Evidence for a Mechanism of Facilitated Diffusion via the Phosphoenolpyruvate:Mannose Phosphotransferase System

Arabinose-Induced Catabolite Repression as a Mechanism for Pentose Hierarchy Control in Clostridium acetobutylicum ATCC 824

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The Bacillus subtilis AraE Protein Displays a Broad Substrate Specificity for Several Different Sugars

Abstract: Bacillus subtilis 168 is unable to grow on xylose and galactose as sole carbon sources, owing to the lack of specific transporters. We show that they are imported into the cell by the activity of AraE, an arabinose transporter whose synthesis is induced by l-arabinose.

Cited by 68 publications

References 14 publications

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Transport of d-Xylose in Lactobacillus pentosus, Lactobacillus casei, andLactobacillus plantarum: Evidence for a Mechanism of Facilitated Diffusion via the Phosphoenolpyruvate:Mannose Phosphotransferase System

Arabinose-Induced Catabolite Repression as a Mechanism for Pentose Hierarchy Control in Clostridium acetobutylicum ATCC 824

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Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon

Characterization of the proteins encoded by theBacillus subtilis yoxA-dacCâ operon