ArticleJournal of bacteriology2009
HPrK regulates succinate-mediated catabolite repression in the gram-negative symbiont Sinorhizobium meliloti.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Regulation of central carbon metabolism and storage polymers by PTSApplied and environmental microbiology · 2026Article
- Endosymbiosis in trypanosomatids: the bacterium regulates the intermediate and oxidative metabolism of the host cell.mSphere · 2025Article
- Comparative genomics reveals insight into the phylogeny and habitat adaptation of novelFrontiers in plant science · 2024Article
- Sequential uptake of aldoses over fructose and enhanced phosphate solubilization in Rhizobium sp. RM.Applied microbiology and biotechnology · 2022Article
- Rhizobial Exopolysaccharides: Genetic Regulation of Their Synthesis and Relevance in Symbiosis with Legumes.International journal of molecular sciences · 2021Review
- Global control of bacterial nitrogen and carbon metabolism by a PTSProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Phototrophic Lactate Utilization byApplied and environmental microbiology · 2019Article
- Sinorhizobium meliloti, a Slow-Growing Bacterium, Exhibits Growth Rate Dependence of Cell Size under Nutrient Limitation.mSphere · 2018Article
- Article
- Genetic Analysis Reveals the Essential Role of Nitrogen Phosphotransferase System Components in Sinorhizobium fredii CCBAU 45436 Symbioses with Soybean and Pigeonpea Plants.Applied and environmental microbiology · 2016Article
- Article
- Biochemical characterization of a nitrogen-type phosphotransferase system reveals that enzyme EI(Ntr) integrates carbon and nitrogen signaling in Sinorhizobium meliloti.Journal of bacteriology · 2014Article
- Expression of the Rhizobium leguminosarum bv. trifolii pssA gene, involved in exopolysaccharide synthesis, is regulated by RosR, phosphate, and the carbon source.Journal of bacteriology · 2013Article
- Members of the Sinorhizobium meliloti ChvI regulon identified by a DNA binding screen.BMC microbiology · 2013Article
- ABC transport is inactivated by the PTS(Ntr) under potassium limitation in Rhizobium leguminosarum 3841.PloS one · 2013Article
- Mutation of the sensor kinase chvG in Rhizobium leguminosarum negatively impacts cellular metabolism, outer membrane stability, and symbiosis.Journal of bacteriology · 2012Article
- Environmental signals and regulatory pathways that influence exopolysaccharide production in rhizobia.International journal of molecular sciences · 2011Review
- Characterization of a two-component regulatory system that regulates succinate-mediated catabolite repression in Sinorhizobium meliloti.Journal of bacteriology · 2010Article
- Functional characterization of the incomplete phosphotransferase system (PTS) of the intracellular pathogen Brucella melitensis.PloS one · 2010Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The HPrK kinase/phosphatase is a common component of the phosphotransferase system (PTS) of gram-positive 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 Delta 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 Delta hprK mutants overproduce exopolysaccharides and form nodules that do not fix nitrogen.
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