2012
Inhibition of Bacterial Virulence: Drug‐Like Molecules Targeting the Salmonella enterica PhoP Response Regulator
Tang YT, Gao R, Havranek JJ, Groisman EA, Stock AM, Marshall GR. Inhibition of Bacterial Virulence: Drug‐Like Molecules Targeting the Salmonella enterica PhoP Response Regulator. Chemical Biology & Drug Design 2012, 79: 1007-1017. PMID: 22339993, PMCID: PMC3445336, DOI: 10.1111/j.1747-0285.2012.01362.x.Peer-Reviewed Original ResearchConceptsTwo-component signal transductionResponse regulatorPhoP response regulatorHistidine kinaseBacterial virulenceGene expressionSensor histidine kinaseVirulence gene regulationSignal transduction systemSignal transduction pathwaysExpression of genesTCST systemsStructure-based virtual screeningGene regulationSignal transductionTranscription factorsTransduction pathwaysTransduction systemVirtual screeningBiophysical assaysAntibacterial developmentMode of actionExternal signalsRegulatorRegulatory systemIntrinsic Negative Feedback Governs Activation Surge in Two-Component Regulatory Systems
Yeo WS, Zwir I, Huang HV, Shin D, Kato A, Groisman EA. Intrinsic Negative Feedback Governs Activation Surge in Two-Component Regulatory Systems. Molecular Cell 2012, 45: 409-421. PMID: 22325356, PMCID: PMC3713471, DOI: 10.1016/j.molcel.2011.12.027.Peer-Reviewed Original Research
2004
Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor
Kato A, Groisman EA. Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor. Genes & Development 2004, 18: 2302-2313. PMID: 15371344, PMCID: PMC517523, DOI: 10.1101/gad.1230804.Peer-Reviewed Original ResearchMeSH KeywordsAllelesBacterial ProteinsBase SequenceGene Expression Regulation, BacterialMagnesiumMolecular Sequence DataPhosphorylationPromoter Regions, GeneticProtein Processing, Post-TranslationalProtein Structure, TertiarySalmonella entericaSignal TransductionTranscription FactorsTranscription, GeneticConceptsTwo-component systemResponse regulatorPhosphorylated formTwo-component regulatory systemTranscription of PmrAResponse regulator PmrAPhoP/PhoQPmrA/PmrBPmrA proteinTarget promotersCognate sensorProtein bindsSignal transductionCellular responsesDephosphorylationRegulatory systemPmrAProteinTranscriptionMultiple signalsRegulatorHigh affinityPmrA.Fundamental questionsPhoP
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
A Signal Transduction System that Responds to Extracellular Iron
Wösten M, Kox L, Chamnongpol S, Soncini F, Groisman E. A Signal Transduction System that Responds to Extracellular Iron. Cell 2000, 103: 113-125. PMID: 11051552, DOI: 10.1016/s0092-8674(00)00092-1.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBinding SitesCarrier ProteinsDrug Resistance, MicrobialExtracellular SpaceGene Expression Regulation, BacterialIronIron-Binding ProteinsPhenotypePolymyxinsProtein Structure, TertiarySalmonella entericaSignal TransductionTranscription FactorsTranscription, GeneticTransferrin-Binding ProteinsConceptsSignal transduction systemTransduction systemTranscription of PmrAWild-type resistancePmrA/PmrBPeriplasmic domainPmrA mutantIron transporterFerritin light chainIron binding proteinAntibiotic polymyxinBinding proteinPmrB proteinIron homeostasisNovel pathwayExtracellular ironIron toxicityProteinVariety of oxidantsLight chainMutantsTranscriptionGenesOrganismsFerric ironAcetyl 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