2021
Limitation of phosphate assimilation maintains cytoplasmic magnesium homeostasis
Bruna RE, Kendra CG, Groisman EA, Pontes MH. Limitation of phosphate assimilation maintains cytoplasmic magnesium homeostasis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2021370118. PMID: 33707210, PMCID: PMC7980370, DOI: 10.1073/pnas.2021370118.Peer-Reviewed Original ResearchConceptsCytoplasmic MgPhosphate assimilationRibosomal RNARegulatory logicP assimilationMolecular basisLoss of viabilityProtein inhibitsPi toxicityAdenosine triphosphateATP synthesisProtein synthesisATP accumulationHomeostasisBacterial growthCytosolic PiDependent processesMagnesium homeostasisBacteriaBiological moleculesInorganic orthophosphateEssential componentAssimilationGrowthRNA
2018
Lvr, a Signaling System That Controls Global Gene Regulation and Virulence in Pathogenic Leptospira
Adhikarla H, Wunder EA, Mechaly AE, Mehta S, Wang Z, Santos L, Bisht V, Diggle P, Murray G, Adler B, Lopez F, Townsend JP, Groisman E, Picardeau M, Buschiazzo A, Ko AI. Lvr, a Signaling System That Controls Global Gene Regulation and Virulence in Pathogenic Leptospira. Frontiers In Cellular And Infection Microbiology 2018, 8: 45. PMID: 29600195, PMCID: PMC5863495, DOI: 10.3389/fcimb.2018.00045.Peer-Reviewed Original ResearchConceptsResponse regulatorTwo-component system proteinsDNA-binding response regulatorGlobal transcriptional regulationHybrid histidine kinaseGlobal gene regulationNovel signal pathwayComprehensive genomic analysisPhosphotransfer assaysTCS genesHistidine kinaseGene duplicationTranscriptional regulationGene regulationCorresponding genesPhylogenetic analysisGenomic analysisMolecular basisMutant strainSystem proteinsSignaling systemInfection processGenesBranched pathwayVirulence
2017
Sequestration from Protease Adaptor Confers Differential Stability to Protease Substrate
Yeom J, Wayne KJ, Groisman EA. Sequestration from Protease Adaptor Confers Differential Stability to Protease Substrate. Molecular Cell 2017, 66: 234-246.e5. PMID: 28431231, PMCID: PMC5424706, DOI: 10.1016/j.molcel.2017.03.009.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBinding, CompetitiveCation Transport ProteinsEndopeptidase ClpGene Expression Regulation, BacterialHalf-LifeModels, MolecularMutationProtein BindingProtein Interaction Domains and MotifsProtein StabilityProteolysisSalmonella typhimuriumStructure-Activity RelationshipSubstrate SpecificityTime FactorsTranscription, GeneticConceptsN-terminal residuesSpecific N-terminal residuesRegulatory protein PhoPN-end ruleProtease ClpAPTemporal transcriptionMgtC geneN-terminusPhoPSpecific substratesClpAPDifferential stabilityProtein levelsGenesMgtCResiduesTranscriptionTerminusProteolysisProteinSubstrateProteaseBacteriaDegradationSequestration
2015
Salmonella promotes virulence by repressing cellulose production
Pontes MH, Lee EJ, Choi J, Groisman EA. Salmonella promotes virulence by repressing cellulose production. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 5183-5188. PMID: 25848006, PMCID: PMC4413311, DOI: 10.1073/pnas.1500989112.Peer-Reviewed Original ResearchConceptsCellulose synthesisWild-type phenotypeWild-type virulenceSalmonella enterica serovar TyphimuriumCyclic diguanylateEnterica serovar TyphimuriumPathogen fitnessAbundant organic polymerMgtC geneAcute virulenceAllosteric activatorAbiotic surfacesMgtC mutantInside macrophagesMutantsVirulence determinantsSerovar TyphimuriumVirulenceCellulose productionEnvironmental insultsCellulose levelsBCSAAttenuated mutantsTraitsDiguanylate
2012
Expression of STM4467-Encoded Arginine Deiminase Controlled by the STM4463 Regulator Contributes to Salmonella enterica Serovar Typhimurium Virulence
Choi Y, Choi J, Groisman EA, Kang DH, Shin D, Ryu S. Expression of STM4467-Encoded Arginine Deiminase Controlled by the STM4463 Regulator Contributes to Salmonella enterica Serovar Typhimurium Virulence. Infection And Immunity 2012, 80: 4291-4297. PMID: 23006851, PMCID: PMC3497419, DOI: 10.1128/iai.00880-12.Peer-Reviewed Original ResearchConceptsCarbamate kinaseOrnithine transcarbamoylaseArginine deiminaseSalmonella enterica Serovar Typhimurium VirulenceBacterium Salmonella enterica serovar TyphimuriumSalmonella enterica serovar TyphimuriumGene functionEnterica serovar TyphimuriumDeletion mutantsMammalian hostsPathway genesRegulatory proteinsADI systemSuccessful infectionTyphimurium virulenceS. typhimuriumMetabolic functionsGenesSerovar TyphimuriumADI activityMurine macrophagesVirulenceMutantsCertain pathogensExpressionControl of a Salmonella virulence locus by an ATP-sensing leader messenger RNA
Lee EJ, Groisman EA. Control of a Salmonella virulence locus by an ATP-sensing leader messenger RNA. Nature 2012, 486: 271-275. PMID: 22699622, PMCID: PMC3711680, DOI: 10.1038/nature11090.Peer-Reviewed Original ResearchMeSH Keywords5' Untranslated RegionsAdenosine TriphosphateAnimalsBacterial ProteinsBase SequenceCation Transport ProteinsFemaleGene Expression Regulation, BacterialHydrogen-Ion ConcentrationMacrophagesMiceMice, Inbred C3HMolecular Sequence DataMutationSalmonella InfectionsSalmonella typhimuriumSequence AlignmentVirulence
2006
Identification 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 constituentsIdentificationAn RNA Sensor for Intracellular Mg2+
Cromie MJ, Shi Y, Latifi T, Groisman EA. An RNA Sensor for Intracellular Mg2+. Cell 2006, 125: 71-84. PMID: 16615891, DOI: 10.1016/j.cell.2006.01.043.Peer-Reviewed Original ResearchMeSH Keywords5' Untranslated RegionsAdenosine TriphosphatasesBacterial ProteinsBiosensing TechniquesConserved SequenceCytoplasmGene Expression Regulation, BacterialMagnesiumMembrane Transport ProteinsModels, GeneticMutationNucleic Acid ConformationOpen Reading FramesPhylogenyPromoter Regions, GeneticRegulatory Sequences, Nucleic AcidRibonucleasesRNA, BacterialRNA, MessengerTerminator Regions, GeneticTranscription, GeneticConceptsMost RNA moleculesDifferent cellular compartmentsStem-loop structureOnly protein componentSalmonella enterica serovar TyphimuriumDifferent stem-loop structuresTransporter MgtAMgtA geneEnterica serovar TyphimuriumMgtA transcriptionRNA polymeraseCellular compartmentsGene transcriptionRNA moleculesTranscription systemUntranslated regionProtein componentsTranscriptionRNA sensorsEnzymatic propertiesSerovar TyphimuriumMgtACytoplasmicDisparate stepsSingular example
2004
Transcriptional Control of the Antimicrobial Peptide Resistance ugtL Gene by the Salmonella PhoP and SlyA Regulatory Proteins*
Shi Y, Latifi T, Cromie MJ, Groisman EA. Transcriptional Control of the Antimicrobial Peptide Resistance ugtL Gene by the Salmonella PhoP and SlyA Regulatory Proteins*. Journal Of Biological Chemistry 2004, 279: 38618-38625. PMID: 15208313, DOI: 10.1074/jbc.m406149200.Peer-Reviewed Original ResearchMeSH KeywordsAntimicrobial Cationic PeptidesBacterial ProteinsBase SequenceBeta-GalactosidaseBinding SitesBlotting, SouthernDeoxyribonuclease IGene Expression Regulation, BacterialMagaininsMagnesiumMembrane ProteinsModels, BiologicalMolecular Sequence DataMutationPeptidesPlasmidsPolymyxin BPromoter Regions, GeneticProtein BindingSalmonellaSingle-Strand Specific DNA and RNA EndonucleasesTranscription FactorsTranscription, GeneticTranscriptional ActivationXenopus ProteinsConceptsPhoP proteinSlyA mutantSlyA proteinPhoP/PhoQTranscription start siteAntimicrobial peptidesTwo-component systemMagainin 2Transcriptional activatorAbility of SalmonellaTranscriptional controlStart siteMaster regulatorRegulatory proteinsTranscriptionVirulence attenuationAntimicrobial peptide magainin 2PhoPGenesProteinPromoterMutantsSlyA.PhoQPeptides
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 questionsControl of the Salmonella ugd gene by three two‐component regulatory systems
Mouslim C, Groisman EA. Control of the Salmonella ugd gene by three two‐component regulatory systems. Molecular Microbiology 2003, 47: 335-344. PMID: 12519186, DOI: 10.1046/j.1365-2958.2003.03318.x.Peer-Reviewed Original Research
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 entericaA small protein that mediates the activation of a two‐component system by another two‐component system
Kox L, Wösten M, Groisman E. A small protein that mediates the activation of a two‐component system by another two‐component system. The EMBO Journal 2000, 19: 1861-1872. PMID: 10775270, PMCID: PMC302009, DOI: 10.1093/emboj/19.8.1861.Peer-Reviewed Original ResearchMeSH KeywordsAnti-Bacterial AgentsBacterial ProteinsBase SequenceDrug Resistance, MicrobialIronMagnesiumModels, BiologicalMolecular Sequence DataMutagenesisMutationPhosphorylationPlasmidsPolymyxinsProtein BindingRecombinant ProteinsRNA Processing, Post-TranscriptionalSalmonella entericaSignal TransductionSingle-Strand Specific DNA and RNA EndonucleasesTranscription FactorsTranscription, GeneticConceptsTwo-component systemTranscription of PmrAPost-transcriptional levelExpression of pmrAPeptide antibiotic polymyxin BPmrD proteinPhoP-PhoQTranscriptional activationGenetic basisHeterologous promoterPmrA-PmrBSmall proteinsGenesPhoP-PhoQ.PmrB proteinAntimicrobial proteinsPhoQ genesProteinPmrAPhoPTranscriptionSalmonella entericaAntibiotic polymyxin BPmrDHigh ironA parallel intraphagosomal survival strategy shared by Mycobacterium tuberculosis and Salmonella enterica
Buchmeier N, Blanc‐Potard A, Ehrt S, Piddington D, Riley L, Groisman E. A parallel intraphagosomal survival strategy shared by Mycobacterium tuberculosis and Salmonella enterica. Molecular Microbiology 2000, 35: 1375-1382. PMID: 10760138, DOI: 10.1046/j.1365-2958.2000.01797.x.Peer-Reviewed Original ResearchConceptsM. tuberculosisIntracellular pathogensMycobacterium tuberculosisSpleens of miceCultured human macrophagesM. tuberculosis mutantsMgtC mutantMacrophage phagosomesTuberculosisSalmonella entericaHuman macrophagesTuberculosis mutantsMacrophagesDifferent diseasesLow magnesiumVirulencePhagosomesMgtC proteinSimilar phenotypeSalmonellaPrevious studiesPathogensLungSpleen
1999
A Salmonella virulence protein that inhibits cellular trafficking
Uchiya K, Barbieri M, Funato K, Shah A, Stahl P, Groisman E. A Salmonella virulence protein that inhibits cellular trafficking. The EMBO Journal 1999, 18: 3924-3933. PMID: 10406797, PMCID: PMC1171468, DOI: 10.1093/emboj/18.14.3924.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBiological TransportCell LineCell SurvivalCytosolEndosomesGenes, BacterialGTP-Binding ProteinsInhibitory Concentration 50Lethal Dose 50LysosomesMacrophagesMembrane FusionMiceMolecular Sequence DataMutationPhagosomesRab5 GTP-Binding ProteinsReceptors, TransferrinSalmonella entericaVirulenceConceptsType III secretion systemSecretion systemIntracellular traffickingSPI-2 pathogenicity islandTrafficking of vesiclesEndosome-endosome fusionHost cell cytosolVirulence proteinsCellular traffickingNormal traffickingSpiC geneCell cytosolPathogenicity islandSalmonella pathogenesisSpiC mutantTraffickingProteinInhibited fusionSindbis virusSalmonella entericaTransferrin receptorJ774 macrophagesMutantsEndosomesGenes
1998
At Least Four Percent of the Salmonella typhimurium Genome Is Required for Fatal Infection of Mice
Bowe F, Lipps C, Tsolis R, Groisman E, Heffron F, Kusters J. At Least Four Percent of the Salmonella typhimurium Genome Is Required for Fatal Infection of Mice. Infection And Immunity 1998, 66: 3372-3377. PMID: 9632607, PMCID: PMC108354, DOI: 10.1128/iai.66.7.3372-3377.1998.Peer-Reviewed Original Research
1997
The Salmonella selC locus contains a pathogenicity island mediating intramacrophage survival
Blanc‐Potard A, Groisman E. The Salmonella selC locus contains a pathogenicity island mediating intramacrophage survival. The EMBO Journal 1997, 16: 5376-5385. PMID: 9311997, PMCID: PMC1170169, DOI: 10.1093/emboj/16.17.5376.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAnimalsBacterial ProteinsBase SequenceCarrier ProteinsCation Transport ProteinsCulture MediaEscherichia coliEscherichia coli ProteinsFemaleGenes, BacterialMacrophagesMagnesiumMembrane Transport ProteinsMiceMice, Inbred BALB CMolecular Sequence DataMultigene FamilyMutationOperonPhenotypeRecombination, GeneticRNA, TransferSalmonella Infections, AnimalSalmonella typhimuriumConceptsPathogenicity islandSelC locusIntramacrophage survivalSalmonella typhimurium chromosomePhoP/PhoQKb DNA segmentVirulence genesNon-pathogenic bacterial speciesTwo-component systemSite of integrationChromosomal clustersTRNA locusVirulence functionsDNA segmentsSalmonella virulenceHomologous regionsMajor regulatorBacterial speciesLociEnteric bacteriaEscherichia coliGenesBenign strainsLow Mg2Virulence
1996
Identification of a pathogenicity island required for Salmonella survival in host cells.
Ochman H, Soncini FC, Solomon F, Groisman EA. Identification of a pathogenicity island required for Salmonella survival in host cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 7800-7804. PMID: 8755556, PMCID: PMC38828, DOI: 10.1073/pnas.93.15.7800.Peer-Reviewed Original ResearchConceptsPathogenicity islandType III secretion systemSalmonella typhimurium chromosomeWild-type levelsEpithelial cell invasionWild-type strainSPI genesSecretion systemPutative regulatorHost cellsSecretory apparatusCell invasionSecreted proteaseVirulence determinantsSpi(-) mutantsGenesProteinProteaseSalmonella survivalEnteric pathogensMutantsChromosomesIslandsCulture supernatantsForms of flagellinMg2+ 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