ArticleProceedings of the National Academy of Sciences of the United States of America2002
Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life?
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.
- Implications of carbon catabolite repression for plant-microbe interactions.Plant communications · 2022Pooled it
- Atypical catabolite repression ofMicrobiology (Reading, England) · 2026Article
- How Bacterial Pathogens Coordinate Appetite with Virulence.Microbiology and molecular biology reviews : MMBR · 2023Review
- HPr prevents FruR-mediated facilitation of RNA polymerase binding to the fru promoter in Vibrio cholerae.Nucleic acids research · 2023Article
- Functional and structural diversification of incomplete phosphotransferase system in cellulose-degrading clostridia.The ISME journal · 2023Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- Intermediary conformations linked to the directionality of the aminoacylation pathway of nonribosomal peptide synthetases.RSC chemical biology · 2021Article
- Bacterial Protein Kinases.Advances in experimental medicine and biology · 2021Article
- Surfactin: A Quorum-Sensing Signal Molecule to Relieve CCR inFrontiers in microbiology · 2020Article
- In-depth analysis of Bacillus subtilis proteome identifies new ORFs and traces the evolutionary history of modified proteins.Scientific reports · 2018Article
- Coordinated regulation of transcription by CcpA and the Staphylococcus aureus two-component system HptRS.PloS one · 2018Article
- Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.Frontiers in microbiology · 2015Article
- The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Microbiology and molecular biology reviews : MMBR · 2014Review
- Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.Virulence · 2014Review
- Metabolic Regulation of a Bacterial Cell System with Emphasis on Escherichia coli Metabolism.ISRN biochemistry · 2013Review
- Carbon catabolite repression in Thermoanaerobacterium saccharolyticum.Biotechnology for biofuels · 2012Article
- CcpA regulates arginine biosynthesis in Staphylococcus aureus through repression of proline catabolism.PLoS pathogens · 2012Article
- Malate-mediated carbon catabolite repression in Bacillus subtilis involves the HPrK/CcpA pathway.Journal of bacteriology · 2011Article
- Functional characterization of the incomplete phosphotransferase system (PTS) of the intracellular pathogen Brucella melitensis.PloS one · 2010Article
- CcpA mediates proline auxotrophy and is required for Staphylococcus aureus pathogenesis.Journal of bacteriology · 2010Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In most Gram-positive bacteria, serine-46-phosphorylated HPr (P-Ser-HPr) controls the expression of numerous catabolic genes ( approximately 10% of their genome) by acting as catabolite corepressor. HPr kinase/phosphorylase (HprK/P), the bifunctional sensor enzyme for catabolite repression, phosphorylates HPr, a phosphocarrier protein of the sugar-transporting phosphoenolpyruvate/glycose phosphotransferase system, in the presence of ATP and fructose-1,6-bisphosphate but dephosphorylates P-Ser-HPr when phosphate prevails over ATP and fructose-1,6-bisphosphate. We demonstrate here that P-Ser-HPr dephosphorylation leads to the formation of HPr and pyrophosphate. HprK/P, which binds phosphate at the same site as the beta phosphate of ATP, probably uses the inorganic phosphate to carry out a nucleophilic attack on the phosphoryl bond in P-Ser-HPr. HprK/P is the first enzyme known to catalyze P-protein dephosphorylation via this phospho-phosphorolysis mechanism. This reaction is reversible, and at elevated pyrophosphate concentrations, HprK/P can use pyrophosphate to phosphorylate HPr. Growth of Bacillus subtilis on glucose increased intracellular pyrophosphate to concentrations ( approximately 6 mM), which in in vitro tests allowed efficient pyrophosphate-dependent HPr phosphorylation. To effectively dephosphorylate P-Ser-HPr when glucose is exhausted, the pyrophosphate concentration in the cells is lowered to 1 mM. In B. subtilis, this might be achieved by YvoE. This protein exhibits pyrophosphatase activity, and its gene is organized in an operon with hprK.
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