2021
RNA chaperone activates Salmonella virulence program during infection
Choi J, Salvail H, Groisman EA. RNA chaperone activates Salmonella virulence program during infection. Nucleic Acids Research 2021, 49: 11614-11628. PMID: 34751407, PMCID: PMC8599858, DOI: 10.1093/nar/gkab992.Peer-Reviewed Original ResearchConceptsPhoP activationVirulence regulator PhoPWild-type virulenceBacterium Salmonella enterica serovar TyphimuriumWild-type S. typhimuriumSalmonella enterica serovar TyphimuriumRNA chaperonesEnterica serovar TyphimuriumRegulator PhoPRedundant proteinsMutant behavesVirulence programVirulence roleS. typhimuriumInside macrophagesSecondary structureSerovar TyphimuriumCritical functionsVirulence genesChaperonesPhoPMutantsRibosomesOrganismsCSPCCellular Adaptations to Cytoplasmic Mg2+ Limitation
Groisman EA, Chan C. Cellular Adaptations to Cytoplasmic Mg2+ Limitation. Annual Review Of Microbiology 2021, 75: 649-672. PMID: 34623895, DOI: 10.1146/annurev-micro-020518-115606.Peer-Reviewed Original ResearchConceptsCytoplasmic MgLeader regionATP-dependent proteaseTranscriptional regulator PhoPAbundant divalent cationOpen reading frameActivity of ribosomesSimilar adaptation strategiesRegulated proteolysisExpression of proteinsRegulator PhoPMicrobial speciesReading frameCellular adaptationDifferent genesCoding regionsBacterial speciesProtein synthesisSpeciesProteinAbundanceDivalent cationsExpressionCytoplasmic Mg2Enzymatic reactionsReduced ATP-dependent proteolysis of functional proteins during nutrient limitation speeds the return of microbes to a growth state
Yeom J, Groisman EA. Reduced ATP-dependent proteolysis of functional proteins during nutrient limitation speeds the return of microbes to a growth state. Science Signaling 2021, 14 PMID: 33500334, PMCID: PMC8378506, DOI: 10.1126/scisignal.abc4235.Peer-Reviewed Original ResearchConceptsATP-dependent proteolysisSlow-growth stateFunctional proteinsGrowth stateATP-dependent proteaseTranscriptional regulator PhoPProtein preservationNutrient limitation conditionsRapid growth statesRegulator PhoPMicrobial strategiesNonfunctional proteinNutrient limitationProtein degradationNitrogen conditionsSame proteaseMagnesium starvationSerovar TyphimuriumProteinLimitation conditionsProteolysisIntracellular ATPParticular nutrientsStationary phaseIntracellular concentration
2005
Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium
Nishino K, Latifi T, Groisman EA. Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium. Molecular Microbiology 2005, 59: 126-141. PMID: 16359323, DOI: 10.1111/j.1365-2958.2005.04940.x.Peer-Reviewed Original ResearchConceptsDrug efflux systemsEfflux systemSalmonella virulenceEscherichia coli homologueToxic compound extrusionResponse regulator PhoPATP-binding cassette (ABC) superfamiliesPhoP/PhoQOuter membrane componentsAmino acid sequenceDrug resistance rolesTwo-component systemSalmonella enterica serovar TyphimuriumGram-negative speciesMultidrug efflux systemsSame operonEnterica serovar TyphimuriumRegulator PhoPCompound extrusionAcid sequenceMajor facilitatorEfflux system genesPromoter regionVirulence phenotypesMajor regulator
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
1995
Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon
Soncini FC, Véscovi EG, Groisman EA. Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon. Journal Of Bacteriology 1995, 177: 4364-4371. PMID: 7543474, PMCID: PMC177185, DOI: 10.1128/jb.177.15.4364-4371.1995.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBase SequenceCloning, MolecularDNA Transposable ElementsGene Expression Regulation, BacterialHomeostasisLac OperonModels, GeneticMolecular Sequence DataMutationNucleic Acid ConformationOperonPromoter Regions, GeneticRNA, BacterialRNA, MessengerSalmonella typhimuriumTranscription FactorsTranscription, GeneticConceptsPhoPQ operonTranscriptional fusionsTranscriptional autoregulationPhoP-PhoQTwo-component regulatory systemAbsence of PhoPTranscriptional regulator PhoPExpression of phoPPhospho-PhoPPhoQ proteinPhoP proteinRegulator PhoPEnvironmental signalsDifferent transcriptsIndependent promotersPosttranscriptional mechanismsOperonPhoPPhoQGenesRegulatory systemBasal levelsProtein levelsProteinPromoter