Molecular characterization of HPr and related enzymes, and regulation of HPr phosphorylation in the ruminal bacterium Streptococcus bovis

Asanuma, Narito; Hino, Tsuneo

doi:10.1007/s00203-003-0516-9

Cited by 16 publications

(17 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cells growing on glucose contained more than half of the HPr as P-Ser-HPr, and the P i concentration was in the low mM range. When glucose was exhausted, P-Ser-HPr disappeared, and the P i concentration went up to 30 mM (26). In in vitro experiments, 20 mM P i completely prevents the phosphorylation of HPr by 5 mM ATP, even when 25 mM FBP is present (177).…”

Section: Characteristics Of Atp-dependent Hpr Phosphorylationmentioning

confidence: 96%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,189

769

View full text Add to dashboard Cite

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.

show abstract

Section: Characteristics Of Atp-dependent Hpr Phosphorylationmentioning

confidence: 96%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,189

769

View full text Add to dashboard Cite

show abstract

“…Therefore, in addition to FBP other metabolites might account for the substrate-dependent differences of HPrK/P activity. Indeed, for Streptococcus bovis, an inverse correlation between HPr(Ser-P) formation and the P i concentration was observed in vivo (1). In addition, other metabolites, such as ATP, acetyl-phosphate, and glyceraldehyde 3-phosphate, were shown to modulate the activity of B. subtilis HPrK/P in vitro (37).…”

Section: Discussionmentioning

confidence: 98%

Carbon Catabolite Repression in Bacillus subtilis : Quantitative Analysis of Repression Exerted by Different Carbon Sources

et al. 2008

View full text Add to dashboard Cite

In many bacteria glucose is the preferred carbon source and represses the utilization of secondary substrates. In Bacillus subtilis, this carbon catabolite repression (CCR) is achieved by the global transcription regulator CcpA, whose activity is triggered by the availability of its phosphorylated cofactors, HPr(Ser46-P) and Crh(Ser46-P). Phosphorylation of these proteins is catalyzed by the metabolite-controlled kinase HPrK/P. Recent studies have focused on glucose as a repressing substrate. Here, we show that many carbohydrates cause CCR. The substrates form a hierarchy in their ability to exert repression via the CcpA-mediated CCR pathway. Of the two cofactors, HPr is sufficient for complete CCR. In contrast, Crh cannot substitute for HPr on substrates that cause a strong repression. Determination of the phosphorylation state of HPr in vivo revealed a correlation between the strength of repression and the degree of phosphorylation of HPr at Ser46. Sugars transported by the phosphotransferase system (PTS) cause the strongest repression. However, the phosphorylation state of HPr at its His15 residue and PTS transport activity have no impact on the global CCR mechanism, which is a major difference compared to the mechanism operative in Escherichia coli. Our data suggest that the hierarchy in CCR exerted by the different substrates is exclusively determined by the activity of HPrK/P.

show abstract

“…HPr can be phosphorylated at the serine-46 residue by the HPr kinase/phosphatase HPrK under energy-replete conditions (33,38,42,47). HPr-Ser46-P, after binding to the transcriptional regulator CcpA, can repress genes associated with secondary carbon source utilization (1,25,47,58). Inducer exclusion is also used by some gram-positive organisms for catabolite repression.…”

mentioning

confidence: 99%

“…In B. subtilis EI phosphorylates HPr at the histidine-15 residue, while HPrK phosphorylates (and dephosphorylates) HPr at the serine-46 (47,48). The latter form of HPr acts as a corepressor of catabolic genes in response to the presence of favored carbon sources (1,25,47,58). Alignment of S. meliloti HPr to HPr proteins of B. subtilis and other bacteria revealed well-conserved regions around Ser-53 and His-22 in the S. meliloti protein that are similar to regions around phosphorylatable serine and histidine residues in other HPr proteins (4).…”

mentioning

confidence: 99%

HPrK Regulates Succinate-Mediated Catabolite Repression in the Gram-Negative SymbiontSinorhizobium meliloti

Pinedo

Gage

2009

J Bacteriol

View full text Add to dashboard Cite

The HPrK kinase/phosphatase is a common component of the phosphotransferase system (PTS) of grampositive bacteria and regulates catabolite repression through phosphorylation/dephosphorylation of its substrate, the PTS protein HPr, at a conserved serine residue. Phosphorylation of HPr by HPrK also affects additional phosphorylation of HPr by the PTS enzyme EI at a conserved histidine residue. Sinorhizobium meliloti can live as symbionts inside legume root nodules or as free-living organisms and is one of the relatively rare gram-negative bacteria known to have a gene encoding HPrK. We have constructed S. meliloti mutants that lack HPrK or that lack key amino acids in HPr that are likely phosphorylated by HPrK and EI. Deletion of hprK in S. meliloti enhanced catabolite repression caused by succinate, as did an S53A substitution in HPr. Introduction of an H22A substitution into HPr alleviated the strong catabolite repression phenotypes of strains carrying ⌬hprK or hpr(S53A) mutations, demonstrating that HPr-His22-P is needed for strong catabolite repression. Furthermore, strains with a hpr(H22A) allele exhibited relaxed catabolite repression. These results suggest that HPrK phosphorylates HPr at the serine-53 residue, that HPr-Ser53-P inhibits phosphorylation at the histidine-22 residue, and that HPr-His22-P enhances catabolite repression in the presence of succinate. Additional experiments show that ⌬hprK mutants overproduce exopolysaccharides and form nodules that do not fix nitrogen.

show abstract

Molecular characterization of HPr and related enzymes, and regulation of HPr phosphorylation in the ruminal bacterium Streptococcus bovis

Cited by 16 publications

References 44 publications

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

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

Carbon Catabolite Repression in Bacillus subtilis : Quantitative Analysis of Repression Exerted by Different Carbon Sources

HPrK Regulates Succinate-Mediated Catabolite Repression in the Gram-Negative SymbiontSinorhizobium meliloti

Contact Info

Product

Resources

About