Regulated expression of HPrK/P does not affect carbon catabolite repression of thexynoperon and ofrocGinBacillus subtilis

Bertram, Ralph; Wünsche, Andrea; Sprehe, Mareen; Hillen, Wolfgang

doi:10.1111/j.1574-6968.2006.00260.x

Cited by 4 publications

(4 citation statements)

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“…In agreement with this assumption, the amount of HprK/P present in B. subtilis cells was reported to have no influence on the ratio of the different HPr forms (59). The amount of HprK/P probably determines only how fast cells can adapt to changes in carbohydrate availability but apparently has no influence on the equilibrium reached under a certain condition.…”

Section: Characteristics Of Atp-dependent Hpr Phosphorylationsupporting

confidence: 62%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

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: Characteristics Of Atp-dependent Hpr Phosphorylationsupporting

confidence: 62%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

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“…XynT belongs to the MFS (Major Facilitator Superfamily) transporter family. The xynT gene was identified as a member of the XylR regulon in C. acetobutylicum (CAC3451) and several Lactobacillales and Bacillales (designated as xynP in B. subtilis by [24]). It is also positionally clustered with xylosidase and xylose pathway genes (Figure 3).…”

Section: Resultsmentioning

confidence: 99%

Reconstruction of xylose utilization pathway and regulons in Firmicutes

et al. 2010

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BackgroundMany Firmicutes bacteria, including solvent-producing clostridia such as Clostridium acetobutylicum, are able to utilize xylose, an abundant carbon source in nature. Nevertheless, homology searches failed to recognize all the genes for the complete xylose and xyloside utilization pathway in most of them. Moreover, the regulatory mechanisms of xylose catabolism in many Firmicutes except Bacillus spp. still remained unclear.ResultsA comparative genomic approach was used to reconstruct the xylose and xyloside utilization pathway and analyze its regulatory mechanisms in 24 genomes of the Firmicutes. A novel xylose isomerase that is not homologous to previously characterized xylose isomerase, was identified in C. acetobutylicum and several other Clostridia species. The candidate genes for the xylulokinase, xylose transporters, and the transcriptional regulator of xylose metabolism (XylR), were unambiguously assigned in all of the analyzed species based on the analysis of conserved chromosomal gene clustering and regulons. The predicted functions of these genes in C. acetobutylicum were experimentally confirmed through a combination of genetic and biochemical techniques. XylR regulons were reconstructed by identification and comparative analysis of XylR-binding sites upstream of xylose and xyloside utilization genes. A novel XylR-binding DNA motif, which is exceptionally distinct from the DNA motif known for Bacillus XylR, was identified in three Clostridiales species and experimentally validated in C. acetobutylicum by an electrophoretic mobility shift assay.ConclusionsThis study provided comprehensive insights to the xylose catabolism and its regulation in diverse Firmicutes bacteria especially Clostridia species, and paved ways for improving xylose utilization capability in C. acetobutylicum by genetic engineering in the future.

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“…, 2006). It is noteworthy that in B. subtilis direct and antisense control exerted by P xyl/tet leads to similar repressed expression levels as demonstrated by Western blots directed against HPr kinase/phosphorylase (HPrK/P), a central player in carbon catabolite regulation in B. subtilis , that was regulated using both approaches (Bertram et al. , 2006).…”

Section: Tet Regulation In Gram‐positive Bacteriamentioning

confidence: 99%

The application of Tet repressor in prokaryotic gene regulation and expression

Bertram

Hillen

2007

Microbial Biotechnology

Self Cite

133

125

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SummaryInducible gene expression based upon Tet repressor (tet regulation) is a broadly applied tool in molecular genetics. In its original environment, Tet repressor (TetR) negatively controls tetracycline (tc) resistance in bacteria. In the presence of tc, TetR is induced and detaches from its cognate DNA sequence tetO, so that a tc antiporter protein is expressed. In this article, we provide a comprehensive overview about tet regulation in bacteria and illustrate the parameters of different regulatory architectures. While some of these set‐ups rely on natural tet‐control regions like those found on transposon Tn10, highly efficient variations of this system have recently been adapted to different Gram‐negative and Gram‐positive bacteria. Novel tet‐controllable artificial or hybrid promoters were employed for target gene expression. They are controlled by regulators expressed at different levels either in a constitutive or in an autoregulated manner. The resulting tetsystems have been used for various purposes. We discuss integrative elements vested with tc‐sensitive promoters, as well as tet regulation in Gram‐negative and Gram‐positive bacteria for analytical purposes and for protein overproduction. Also the use of TetR as an in vivo biosensor for tetracyclines or as a regulatory device in synthetic biology constructs is outlined. Technical specifications underlying different regulatory set‐ups are highlighted, and finally recent developments concerning variations of TetR are presented, which may expand the use of prokaryotic tet systems in the future.

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Regulated expression of HPrK/P does not affect carbon catabolite repression of thexynoperon and ofrocGinBacillus subtilis

Cited by 4 publications

References 28 publications

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

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

Reconstruction of xylose utilization pathway and regulons in Firmicutes

The application of Tet repressor in prokaryotic gene regulation and expression

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