2013
The Biology of the PmrA/PmrB Two-Component System: The Major Regulator of Lipopolysaccharide Modifications
Chen HD, Groisman EA. The Biology of the PmrA/PmrB Two-Component System: The Major Regulator of Lipopolysaccharide Modifications. Annual Review Of Microbiology 2013, 67: 83-112. PMID: 23799815, PMCID: PMC8381567, DOI: 10.1146/annurev-micro-092412-155751.Peer-Reviewed Original ResearchConceptsPmrA/PmrBTwo-component systemPmrA/PmrB systemMajor regulatorEnteric pathogen Salmonella entericaGene expression outputPathogen Salmonella entericaTranscriptional regulatorsExpression outputEcological nichesOuter membraneRelated bacteriaLPS modificationsExtent bacteriaLipopolysaccharide modificationDifferential survivalRegulatorHost immune systemNegative bacteriaSalmonella entericaBacteriaBiologyPmrBQuantitative differencesImmune system
2011
Ancestral Genes Can Control the Ability of Horizontally Acquired Loci to Confer New Traits
Chen HD, Jewett MW, Groisman EA. Ancestral Genes Can Control the Ability of Horizontally Acquired Loci to Confer New Traits. PLOS Genetics 2011, 7: e1002184. PMID: 21811415, PMCID: PMC3140997, DOI: 10.1371/journal.pgen.1002184.Peer-Reviewed Original ResearchMeSH KeywordsAnti-Bacterial AgentsBacterial ProteinsDNA, BacterialDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGene Transfer, HorizontalKineticsMagnesiumMolecular Sequence DataPhosphorylationPolymyxin BReverse Transcriptase Polymerase Chain ReactionSalmonella typhimuriumSequence Analysis, DNATranscription FactorsTransformation, BacterialConceptsGene productsPmrD proteinPmrA/PmrB systemSpecies-specific traitsPmrA/PmrBE. coliHigh phosphatase activityBacterium Escherichia coliTwo-component systemPmrA proteinPolymyxin B resistanceAncestral locusAncestral proteinAncestral geneAncestral pathwayNew traitsBiochemical activityDifferent speciesGenesPmrB proteinEscherichia coliPhosphatase activityB resistanceProteinSalmonella enterica
2006
Acid pH activation of the PmrA/PmrB two‐component regulatory system of Salmonella enterica
Perez JC, Groisman EA. Acid pH activation of the PmrA/PmrB two‐component regulatory system of Salmonella enterica. Molecular Microbiology 2006, 63: 283-293. PMID: 17229213, PMCID: PMC1804205, DOI: 10.1111/j.1365-2958.2006.05512.x.Peer-Reviewed Original ResearchConceptsGlutamic acid residuesPmrA/PmrB systemAcid residuesTwo-component regulatory systemPathogen Salmonella enterica serovar TyphimuriumResponse regulator PmrATranscription of genesPmrA/PmrBSalmonella enterica serovar TyphimuriumPmrA proteinPolymyxin B resistancePeriplasmic domainWild-type SalmonellaEnterica serovar TyphimuriumGene productsGene expressionAnimal hostsRegulatory systemB resistanceSerovar TyphimuriumTranscriptionSalmonella entericaCellular changesGenesPH activationIdentification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
Nishino K, Hsu FF, Turk J, Cromie MJ, Wösten MM, Groisman EA. Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III). Molecular Microbiology 2006, 61: 645-654. PMID: 16803591, PMCID: PMC1618816, DOI: 10.1111/j.1365-2958.2006.05273.x.Peer-Reviewed Original ResearchMeSH KeywordsAluminumBacterial ProteinsBase SequenceDrug Resistance, BacterialEscherichia coli ProteinsGene Expression Regulation, BacterialIronLipid ALipopolysaccharidesMolecular Sequence DataMutationPeriplasmPhosphoric Monoester HydrolasesPhosphorylationPolymyxin BSalmonella typhimuriumSoil MicrobiologyTranscription FactorsConceptsPmrA/PmrB systemGram-negative bacterial speciesNon-host environmentsPmrA/PmrBWild-type strainSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumOuter membraneLipopolysaccharide modificationBacterial speciesCovalent modificationResistance genesSerovar TyphimuriumOxygen-dependent killingPmrAEssential metalsHomeostatic mechanismsSalmonella survivalMutantsDephosphorylationGenesSpeciesProteinMajor constituentsIdentificationThe PmrA/PmrB and RcsC/YojN/RcsB systems control expression of the Salmonella O‐antigen chain length determinant
Delgado MA, Mouslim C, Groisman EA. The PmrA/PmrB and RcsC/YojN/RcsB systems control expression of the Salmonella O‐antigen chain length determinant. Molecular Microbiology 2006, 60: 39-50. PMID: 16556219, DOI: 10.1111/j.1365-2958.2006.05069.x.Peer-Reviewed Original ResearchConceptsPmrA/PmrBO-antigen subunitSame start siteHydrophobic lipid ASDS/PAGE gelsChain length determinantTwo-component systemSalmonella enterica serovar TyphimuriumO-antigenGram-negative bacteriaNull mutantsEnterica serovar TyphimuriumStart siteRcsB mutantDifferent environmental conditionsCell envelopeRegulatory proteinsLPS genesOutermost componentCore oligosaccharideSerovar TyphimuriumGenesEnvironmental conditionsPAGE gelsRcsB
2005
Transcriptional Regulation of the 4-Amino-4-deoxy-L-arabinose Biosynthetic Genes in Yersinia pestis *
Winfield MD, Latifi T, Groisman EA. Transcriptional Regulation of the 4-Amino-4-deoxy-L-arabinose Biosynthetic Genes in Yersinia pestis *. Journal Of Biological Chemistry 2005, 280: 14765-14772. PMID: 15710615, DOI: 10.1074/jbc.m413900200.Peer-Reviewed Original ResearchMeSH KeywordsAmino SugarsBacterial ProteinsBase SequenceBinding SitesCell ProliferationDeoxyribonuclease IDNA PrimersGene DeletionGene Expression Regulation, BacterialIronLipid AMagnesiumModels, BiologicalMolecular Sequence DataPlasmidsPolymyxin BPromoter Regions, GeneticSalmonella entericaSingle-Strand Specific DNA and RNA EndonucleasesTranscription FactorsTranscription, GeneticYersinia pestisConceptsPmrD proteinBiosynthetic genesPhoP/PhoQ systemTwo-component regulatory systemTranscription of PmrADisparate regulatory pathwaysYersinia pestisRelated bacterial speciesPmrA/PmrBSalmonella enterica serovar TyphimuriumPmrA proteinPhoP proteinGram-negative bacteriaTranscriptional regulationUgd geneMembrane remodelingEnterica serovar TyphimuriumRegulatory pathwaysCationic antimicrobial peptidesDistinct binding sitesBacterial membranesBacterial speciesDifferent promotersGenesPmrB protein
2004
Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes
Winfield MD, Groisman EA. Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 17162-17167. PMID: 15569938, PMCID: PMC534605, DOI: 10.1073/pnas.0406038101.Peer-Reviewed Original ResearchConceptsPmrD proteinPolymyxin B resistanceHomologous genesB resistancePhenotypic differencesDifferential regulationRange of nichesSpecies-specific genesPmrA/PmrBE. coliE. coli KTwo-component systemEnterica serovar TyphimuriumGene transcriptionS. enterica serovar TyphimuriumEcological consequencesColi KLPS modificationsNatural isolatesPathogenicity islandE. coli strainsGenesMolecular analysisEscherichia coliSerovar TyphimuriumConnecting 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
Signal-dependent Requirement for the Co-activator Protein RcsA in Transcription of the RcsB-regulated ugd Gene*
Mouslim C, Latifi T, Groisman EA. Signal-dependent Requirement for the Co-activator Protein RcsA in Transcription of the RcsB-regulated ugd Gene*. Journal Of Biological Chemistry 2003, 278: 50588-50595. PMID: 14514676, DOI: 10.1074/jbc.m309433200.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBase SequenceBeta-GalactosidaseBinding SitesChromosomesDeoxyribonuclease IEscherichia coli ProteinsGene DeletionIronMagnesiumModels, BiologicalModels, GeneticMolecular Sequence DataMutationPeriplasmic ProteinsPlasmidsPromoter Regions, GeneticSalmonellaSequence Homology, Amino AcidSingle-Strand Specific DNA and RNA EndonucleasesTemperatureTranscription FactorsTranscription, GeneticConceptsUgd genePmrA/PmrB systemTwo-component systems PhoP/PhoQS1 mapping experimentsPhoP/PhoQPmrA/PmrBUDP-glucose dehydrogenasePhoP proteinPhosphorelay systemIndependent transcriptionVariety of signalsPmrA mutantMembrane proteinsSame promoterCps operonRcsBGene expressionRcsATranscriptionGenesMapping experimentsCps transcriptionPhoPPromoterLow Mg2Closing the loop: The PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD
Kato A, Latifi T, Groisman EA. Closing the loop: The PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 4706-4711. PMID: 12676988, PMCID: PMC153620, DOI: 10.1073/pnas.0836837100.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceArtificial Gene FusionBacterial ProteinsBase SequenceBinding SitesDNA, BacterialFeedbackGene Expression Regulation, BacterialGenes, BacterialModels, GeneticMolecular Sequence DataMutationPlasmidsPromoter Regions, GeneticProtein BindingSalmonella typhimuriumTranscription FactorsConceptsPmrA proteinTwo-component systemResponse regulator PmrAAppropriate cellular responsesPmrA/PmrBPhoQ proteinPhoP proteinRegulatory circuitsPosttranscriptional levelPromoter upstreamNegative regulationCellular responsesPmrB proteinCellular levelProteinPmrASalmonella entericaGenesMultiple signalsPmrDFeedback loopSingular exampleExpressionPhoPFundamental questions
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 iron
1999
Molecular Characterization of the PmrA Regulon*
Wösten M, Groisman E. Molecular Characterization of the PmrA Regulon*. Journal Of Biological Chemistry 1999, 274: 27185-27190. PMID: 10480935, DOI: 10.1074/jbc.274.38.27185.Peer-Reviewed Original Research