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
2020
How Pathogens Feel and Overcome Magnesium Limitation When in Host Tissues
Blanc-Potard AB, Groisman EA. How Pathogens Feel and Overcome Magnesium Limitation When in Host Tissues. Trends In Microbiology 2020, 29: 98-106. PMID: 32807623, PMCID: PMC7855738, DOI: 10.1016/j.tim.2020.07.003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCation Transport ProteinsHost-Pathogen InteractionsHumansMacrophagesMagnesiumSalmonella InfectionsSalmonella typhimuriumConceptsNutritional immunityHost cell compartmentsAbundant divalent cationHost tissuesSalmonella enterica serovar TyphimuriumAvailability of nutrientsPathogen responseEnterica serovar TyphimuriumMacrophage proteinHost organismLiving cellsMagnesium limitationAmino acidsIntracellular pathogensSerovar TyphimuriumNutrient concentrationsCell compartmentPathogensDivalent cationsNutrientsMagnesium deprivationEssentialityOrganismsCytoplasmProteinSmall proteins regulate Salmonella survival inside macrophages by controlling degradation of a magnesium transporter
Yeom J, Shao Y, Groisman EA. Small proteins regulate Salmonella survival inside macrophages by controlling degradation of a magnesium transporter. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 20235-20243. PMID: 32753384, PMCID: PMC7443967, DOI: 10.1073/pnas.2006116117.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCation Transport ProteinsCell LineMacrophagesMagnesiumMicePlasmidsSalmonella typhimuriumVirulenceConceptsSmall proteinsAmino acid identityFacultative intracellular pathogenTransporter MgtAProtease FtsHMagnesium transportersAcid identityMacrophage proteinRelated transportersSame transcriptPathogen survivalMgtBIntracellular pathogensSerovar TyphimuriumProteinLimitation conditionsHost tissuesMgtROxidative stressTransportersSalmonella survivalSingular exampleFtsHMacrophagesMgtA
2018
Protein synthesis controls phosphate homeostasis
Pontes MH, Groisman EA. Protein synthesis controls phosphate homeostasis. Genes & Development 2018, 32: 79-92. PMID: 29437726, PMCID: PMC5828397, DOI: 10.1101/gad.309245.117.Peer-Reviewed Original ResearchConceptsPi starvation responsesStarvation responseProtein synthesisPi transporter genesProtein synthesis controlATP consumptionPi starvationRegulatory connectionsPi homeostasisTransporter geneExtracellular milieuCytoplasmic MgCytoplasmic PiSerovar TyphimuriumPharmacological inhibitionATP levelsRibosomesCytoplasmic magnesiumBacteriumHomeostasisSynthesis controlPhoBSaccharomycesTranscriptionYeast
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
2016
RNA secondary structures regulate three steps of Rho-dependent transcription termination within a bacterial mRNA leader
Kriner MA, Groisman EA. RNA secondary structures regulate three steps of Rho-dependent transcription termination within a bacterial mRNA leader. Nucleic Acids Research 2016, 45: 631-642. PMID: 28123036, PMCID: PMC5314796, DOI: 10.1093/nar/gkw889.Peer-Reviewed Original Research
2015
The Bacterial Transcription Termination Factor Rho Coordinates Mg2+ Homeostasis with Translational Signals
Kriner MA, Groisman EA. The Bacterial Transcription Termination Factor Rho Coordinates Mg2+ Homeostasis with Translational Signals. Journal Of Molecular Biology 2015, 427: 3834-3849. PMID: 26523680, PMCID: PMC4964609, DOI: 10.1016/j.jmb.2015.10.020.Peer-Reviewed Original ResearchMeSH Keywords5' Untranslated RegionsAmino Acid SequenceBacterial ProteinsBase SequenceCation Transport ProteinsGene Expression Regulation, BacterialHomeostasisInverted Repeat SequencesMagnesiumMolecular Sequence DataNucleic Acid ConformationProtein BiosynthesisRho FactorSalmonella typhimuriumTranscription Initiation SiteConceptsLeader regionTranslational signalsGenome-wide activityShort open reading framesRho utilization siteRho-dependent terminationRho-dependent terminatorsOpen reading frameSalmonella enterica serovar TyphimuriumNascent RNATranscription terminationEnterica serovar TyphimuriumTransport genesProtein RhoRNA polymeraseReading frameLeader mRNASpecific genesRNA conformationEfficient translationExclusive conformationsTranscriptionSerovar TyphimuriumGenesRhoFlagella-independent surface motility in Salmonella enterica serovar Typhimurium
Park SY, Pontes MH, Groisman EA. Flagella-independent surface motility in Salmonella enterica serovar Typhimurium. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 1850-1855. PMID: 25624475, PMCID: PMC4330729, DOI: 10.1073/pnas.1422938112.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsBase SequenceCation Transport ProteinsComputational BiologyFlagellaGene Expression Regulation, BacterialMagnesiumMembrane Transport ProteinsMitochondrial Proton-Translocating ATPasesMolecular Sequence DataMovementMutagenesisSalmonella typhimuriumSequence AlignmentSequence Analysis, DNAConceptsSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumPhoP/PhoQ regulatory systemMgtC mutantFlagellum-independent mannerFlagella-mediated motilitySerovar TyphimuriumForm of motilityWild-type SalmonellaNull mutantsMultiprotein complexesMgtC proteinF1Fo-ATPaseHeterologous promoterSmall proteinsUnknown functionProteinase K treatmentSurface motilityMgtAMutantsGroup motilityAllelic formsRegulatory systemBacterial replicationGenes
2014
Control of a Salmonella virulence operon by proline-charged tRNAPro
Lee EJ, Choi J, Groisman EA. Control of a Salmonella virulence operon by proline-charged tRNAPro. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 3140-3145. PMID: 24516160, PMCID: PMC3939920, DOI: 10.1073/pnas.1316209111.Peer-Reviewed Original Research5' Untranslated RegionsAmino Acid SequenceAnimalsBacterial ProteinsBase PairingBase SequenceCation Transport ProteinsCodonGene Expression Regulation, BacterialHost-Pathogen InteractionsMiceMolecular Sequence DataOligodeoxyribonucleotidesOpen Reading FramesProlineReal-Time Polymerase Chain ReactionRNA, Transfer, ProSalmonella typhimuriumVirulence
2013
A Bacterial Virulence Protein Promotes Pathogenicity by Inhibiting the Bacterium’s Own F1Fo ATP Synthase
Lee EJ, Pontes MH, Groisman EA. A Bacterial Virulence Protein Promotes Pathogenicity by Inhibiting the Bacterium’s Own F1Fo ATP Synthase. Cell 2013, 154: 146-156. PMID: 23827679, PMCID: PMC3736803, DOI: 10.1016/j.cell.2013.06.004.Peer-Reviewed Original Research
2012
Tandem attenuators control expression of the Salmonella mgtCBR virulence operon
Lee EJ, Groisman EA. Tandem attenuators control expression of the Salmonella mgtCBR virulence operon. Molecular Microbiology 2012, 86: 212-224. PMID: 22857388, PMCID: PMC3641672, DOI: 10.1111/j.1365-2958.2012.08188.x.Peer-Reviewed Original ResearchControl 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
2010
An antisense RNA that governs the expression kinetics of a multifunctional virulence gene
Lee EJ, Groisman EA. An antisense RNA that governs the expression kinetics of a multifunctional virulence gene. Molecular Microbiology 2010, 76: 1020-1033. PMID: 20398218, PMCID: PMC2909850, DOI: 10.1111/j.1365-2958.2010.07161.x.Peer-Reviewed Original ResearchConceptsAntisense RNAGenome-wide transcriptome analysisRegulatory protein PhoPLong antisense RNAProtein levelsAntisense transcriptionMgtC proteinTranscriptome analysisRNase EAntisense transcriptsPolycistronic messageRNase IIISalmonella virulenceBacterial speciesPhysiological roleExpression kineticsTranscriptionRNAVirulence genesApparent roleVirulencePhoPSalmonella entericaMgtCAmgRS
2009
Activated by Different Signals, the PhoP/PhoQ Two-Component System Differentially Regulates Metal Uptake
Choi E, Groisman EA, Shin D. Activated by Different Signals, the PhoP/PhoQ Two-Component System Differentially Regulates Metal Uptake. Journal Of Bacteriology 2009, 191: 7174-7181. PMID: 19801407, PMCID: PMC2786564, DOI: 10.1128/jb.00958-09.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesBacterial ProteinsBiological TransportBlotting, WesternCation Transport ProteinsGene Expression Regulation, BacterialHydrogen-Ion ConcentrationMagnesiumMembrane Transport ProteinsMetalsPhosphorylationReverse Transcriptase Polymerase Chain ReactionSalmonella typhimuriumConceptsPhoP/PhoQ systemPhoP/PhoQTwo-component systemTwo-component regulatory systemMgtA genePhoP proteinVirulence functionsMgtA transcriptionSalmonella genesLeader regionTransporter geneBiological consequencesGenesRegulatory systemAntimicrobial peptidesDistinct setsPhoQTranscriptionMetal uptakeSalmonella entericaMultiple signalsProteinExpressionPhoPMgtA
2002
Mg2+ homeostasis and avoidance of metal toxicity
Chamnongpol S, Groisman EA. Mg2+ homeostasis and avoidance of metal toxicity. Molecular Microbiology 2002, 44: 561-571. PMID: 11972791, DOI: 10.1046/j.1365-2958.2002.02917.x.Peer-Reviewed Original ResearchConceptsPhoP/PhoQ systemPhoP mutantPresence of PhoPGram-negative bacterium Salmonella entericaPhoP/PhoQBacterium Salmonella entericaTwo-component systemCorA geneCellular functionsMutantsMetal toxicityProtein levelsIntracellular levelsPhoPMgtATranscriptionSalmonella entericaMgtBLow Mg2Levels of Mg2CorAIron accumulationPhoQUncontrolled influxUptake
2000
A 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
The SPI-3 Pathogenicity Island ofSalmonella enterica
Blanc-Potard A, Solomon F, Kayser J, Groisman E. The SPI-3 Pathogenicity Island ofSalmonella enterica. Journal Of Bacteriology 1999, 181: 998-1004. PMID: 9922266, PMCID: PMC93469, DOI: 10.1128/jb.181.3.998-1004.1999.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdhesins, Escherichia coliAmino Acid SequenceBacterial ProteinsBase CompositionCarrier ProteinsCation Transport ProteinsChromosomes, BacterialDNA PrimersDNA-Binding ProteinsEscherichia coliEvolution, MolecularMolecular Sequence DataMultigene FamilyOpen Reading FramesOperonPhylogenyPolymerase Chain ReactionRNA, BacterialRNA, TransferSalmonella entericaSequence AlignmentTranscription FactorsTranscription, GeneticVibrio choleraeVirulenceConceptsOpen reading framePathogenicity islandReading framePathogen-specific virulence genesSubspecies of SalmonellaFour-gene clusterMolecular genetic structureSalmonella enterica serovar TyphimuriumGenetic structureTranscriptional unitsChromosomal clustersEnterica serovar TyphimuriumTRNA locusSequence similaritySalmonella genomeRegulatory proteinsEnteropathogenic Escherichia coliSPI-3Escherichia coliSerovar TyphimuriumInsertion sequenceVibrio choleraeVirulence genesMultistep processSubspecies
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
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 fusion