2004
Signal-dependent Binding of the Response Regulators PhoP and PmrA to Their Target Promoters in Vivo *
Shin D, Groisman EA. Signal-dependent Binding of the Response Regulators PhoP and PmrA to Their Target Promoters in Vivo *. Journal Of Biological Chemistry 2004, 280: 4089-4094. PMID: 15569664, DOI: 10.1074/jbc.m412741200.Peer-Reviewed Original ResearchConceptsResponse regulator PhoPPmrA proteinPhoP proteinRegulator PhoPTranscription of PhoPWild-type strainTarget promotersPromoter occupancyChromatin immunoprecipitationPromotes phosphorylationRegulatory regionsTarget genesPhoPValine residueLow Mg2GenesPhosphorylationPromoterProteinAsp 52TranscriptionSalmonella entericaVivoImmunoprecipitationMg2
2003
Mg2+ Sensing by the Mg2+ Sensor PhoQ of Salmonella enterica
Chamnongpol S, Cromie M, Groisman EA. Mg2+ Sensing by the Mg2+ Sensor PhoQ of Salmonella enterica. Journal Of Molecular Biology 2003, 325: 795-807. PMID: 12507481, DOI: 10.1016/s0022-2836(02)01268-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBase SequenceBinding SitesConserved SequenceDNA, BacterialMagnesiumMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein Structure, TertiaryRecombinant ProteinsSalmonella entericaSequence Homology, Amino AcidTranscription, GeneticConceptsTranscription of PhoPPhoQ proteinSensor PhoQPeriplasmic domainTwo-component regulatory systemResponse regulator PhoPExpression of phoPPhoP/PhoQWild-type responseWild-type abilityAmino acid residuesGram-negative speciesRegulator PhoPGene transcriptionPhoPAcid residuesTranscriptionHistidine residuesPhoQGenesAcetyl phosphateRegulatory systemProteinMutantsSalmonella enterica
2000
Acetyl phosphate-dependent activation of a mutant PhoP response regulator that functions independently of its cognate sensor kinase11Edited by M. Gottesman
Chamnongpol S, Groisman E. Acetyl phosphate-dependent activation of a mutant PhoP response regulator that functions independently of its cognate sensor kinase11Edited by M. Gottesman. Journal Of Molecular Biology 2000, 300: 291-305. PMID: 10873466, DOI: 10.1006/jmbi.2000.3848.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SubstitutionBacterial ProteinsEnvironmentGene Expression Regulation, BacterialGenes, BacterialGenes, RegulatorMagnesiumMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsModels, MolecularMutationOperonOrganophosphatesPhosphorylationProtein BindingProtein BiosynthesisProtein Structure, TertiaryRecombinant Fusion ProteinsSalmonella entericaTrans-ActivatorsTranscription, GeneticConceptsTranscription of PhoPResponse regulatorAcetyl phosphateResponse regulator receiver domainSites of phosphorylationVirulence gene expressionPhoP response regulatorTwo-component systemPhoQ proteinPhoP proteinReceiver domainSensor kinaseTranscriptional repressionCognate sensorMutant proteinsM. GottesmanPhosphorylated stateAspartate residueGene expressionPhoPTranscriptionPhosphate donorRegulatorProteinSalmonella enterica
1997
Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+ *
Véscovi E, Ayala Y, Di Cera E, Groisman E. Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+ *. Journal Of Biological Chemistry 1997, 272: 1440-1443. PMID: 8999810, DOI: 10.1074/jbc.272.3.1440.Peer-Reviewed Original ResearchConceptsTranscription of PhoPPhoQ proteinDistinct binding sitesTwo-component regulatory systemGram-negative bacterium Salmonella typhimuriumPhoP/PhoQSingle amino acid substitutionBacterium Salmonella typhimuriumTryptophan intrinsic fluorescenceBinding sitesAmino acid substitutionsPeriplasmic domainAcid polypeptide
1996
Molecular basis of the magnesium deprivation response in Salmonella typhimurium: identification of PhoP-regulated genes
Soncini FC, Véscovi E, Solomon F, Groisman EA. Molecular basis of the magnesium deprivation response in Salmonella typhimurium: identification of PhoP-regulated genes. Journal Of Bacteriology 1996, 178: 5092-5099. PMID: 8752324, PMCID: PMC178303, DOI: 10.1128/jb.178.17.5092-5099.1996.Peer-Reviewed Original ResearchConceptsTranscription of PhoPPhoP-dependent mannerOpen reading frameLac gene fusionsWild-type strainPhoP-PhoQ systemTwo-component systemUDP-glucose dehydrogenaseSequence similarityPhoP-PhoQPhoPQ operonReading frameDeprivation responseFusion strainMolecular basisSalmonella typhimuriumPhoPDifferent proteinsSolid mediumGene fusionsUptake systemGenesNormal growthMgtASuch fusionMg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence
Véscovi E, Soncini F, Groisman E. Mg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence. Cell 1996, 84: 165-174. PMID: 8548821, DOI: 10.1016/s0092-8674(00)81003-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBase SequenceCationsGene Expression Regulation, BacterialHydrogen-Ion ConcentrationKineticsMagnesiumMolecular Sequence DataMutationPeptidesPhenotypeProtein ConformationSalmonella typhimuriumSensitivity and SpecificitySignal TransductionTranscription FactorsVirulenceConceptsPhoP/PhoQ systemTranscription of PhoPSignal transduction cascadeVirulence regulatory systemGene expression patternsPeriplasmic domainWild-type SalmonellaExtracellular signalsTransduction cascadeSalmonella virulenceExpression patternsFirst messengersPhoPRegulatory systemGenesPhoQSalmonella typhimuriumPhysiological concentrationsDivalent cationsTranscriptionConcentration of Mg2LociMg2DomainVirulence