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
An RNA motif advances transcription by preventing Rho-dependent termination
Sevostyanova A, Groisman EA. An RNA motif advances transcription by preventing Rho-dependent termination. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: e6835-e6843. PMID: 26630006, PMCID: PMC4687561, DOI: 10.1073/pnas.1515383112.Peer-Reviewed Original ResearchConceptsRho-dependent transcription terminationTranscription terminationRNA elementsNucleic Acid Binding ProteinsRho-dependent terminationOpen reading frameRNA polymeraseReading frameBacterial RNALeader regionRNA motifsRNA conformationRho's accessInefficient translationBinding proteinInactive complexPharmacological inhibitionRhoTranscriptionThe 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
2012
Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems
Townsend GE, Raghavan V, Zwir I, Groisman EA. Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 110: e161-e169. PMID: 23256153, PMCID: PMC3545799, DOI: 10.1073/pnas.1212102110.Peer-Reviewed Original ResearchConceptsTwo-component regulatory systemResponse regulatorSensor kinasePhosphotransfer specificityRelaxed specificityTwo-component systemHuman gut symbiont Bacteroides thetaiotaomicronGut symbiont Bacteroides thetaiotaomicronRR pairsCognate response regulatorCognate protein partnersRegulatory systemProtein partnersTransduce signalsCellular processesSignal transductionSingle polypeptidePhosphoryl transferNoncognate proteinsBacteroides thetaiotaomicronSpecific interactionsRegulatorIntramolecular arrangementTransductionKinase
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
Identifying promoter features of co-regulated genes with similar network motifs
Harari O, del Val C, Romero-Zaliz R, Shin D, Huang H, Groisman EA, Zwir I. Identifying promoter features of co-regulated genes with similar network motifs. BMC Bioinformatics 2009, 10: s1. PMID: 19426448, PMCID: PMC2681069, DOI: 10.1186/1471-2105-10-s4-s1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesComputational BiologyDNA-Directed RNA PolymerasesEscherichia coliGene Expression Regulation, BacterialGene Regulatory NetworksGenome, BacterialMolecular Sequence DataPromoter Regions, GeneticRegulatory Sequences, Nucleic AcidSalmonella typhiTranscription FactorsConceptsTranscriptional regulatorsPromoter featuresNetwork motifsTranscription factorsTarget genesRegulatory proteinsPhoP/PhoQ regulatory systemExpression patternsGene expressionCo-regulated genesGroup of genesGene regulatory networksDifferential gene expressionCis-acting elementsDifferent expression patternsCharacteristic expression patternsSalmonella enterica serovar TyphimuriumProteobacterial genomesPhoP proteinEnterica serovar TyphimuriumRegulatory networksRNA polymeraseRegulatory regionsRepression siteMultiple promoters
2004
Type III Secretion System Genes in Clinical Aeromonas Isolates
Chacón MR, Soler L, Groisman EA, Guarro J, Figueras MJ. Type III Secretion System Genes in Clinical Aeromonas Isolates. Journal Of Clinical Microbiology 2004, 42: 1285-1287. PMID: 15004096, PMCID: PMC356863, DOI: 10.1128/jcm.42.3.1285-1287.2004.Peer-Reviewed Original Research
2003
The Salmonella SpiC protein targets the mammalian Hook3 protein function to alter cellular trafficking
Shotland Y, Krämer H, Groisman EA. The Salmonella SpiC protein targets the mammalian Hook3 protein function to alter cellular trafficking. Molecular Microbiology 2003, 49: 1565-1576. PMID: 12950921, DOI: 10.1046/j.1365-2958.2003.03668.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsCell LineCyclic AMPGenes, ReporterLysosomesMacrophagesMiceMicroscopy, FluorescenceMicrotubule-Associated ProteinsMolecular Sequence DataPhagosomesProtein BindingProtein TransportRecombinant Fusion ProteinsSalmonella typhimuriumSequence Homology, Amino AcidConceptsPhagosome-lysosome fusionCellular traffickingType III secretion systemEndosome-endosome fusionDominant negative mutantCytosol of macrophagesMammalian proteinsPhenotype of cellsProtein functionGolgi morphologySecretion systemDistribution of lysosomesSpiC genePhagosomal membraneProteinMurine macrophagesTraffickingCytosolVero cellsMacrophagesCellsMutantsHook3FusionGenesClosing 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 questionsMg2+ 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
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 macrophagesMutantsEndosomesGenesA Periplasmicd-Alanyl-d-Alanine Dipeptidase in the Gram-Negative Bacterium Salmonella enterica
Hilbert F, del Portillo F, Groisman E. A Periplasmicd-Alanyl-d-Alanine Dipeptidase in the Gram-Negative Bacterium Salmonella enterica. Journal Of Bacteriology 1999, 181: 2158-2165. PMID: 10094694, PMCID: PMC93629, DOI: 10.1128/jb.181.7.2158-2165.1999.Peer-Reviewed Original ResearchConceptsD-alanyl-D-alanine dipeptidaseD-Ala-D-Ala dipeptidaseHorizontal gene transferRelated bacterial speciesSpecies Salmonella entericaEscherichia coli KSimilar substrate specificityBacterium Salmonella entericaSalmonella entericaDipeptidase geneWild-type SalmonellaPeptidoglycan metabolismSole carbon sourcePeriplasmic spaceSalmonella chromosomeSubstrate specificityD-AlaColi KBacterial speciesSalmonella enzymeVanX proteinGene transferEnzymatic activityGlycopeptide antibiotic vancomycinCarbon sourceThe 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
Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+ *
Véscovi E, Ayala Y, Di Cera E, Groisman E. Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+ *. Journal Of Biological Chemistry 1997, 272: 1440-1443. PMID: 8999810, DOI: 10.1074/jbc.272.3.1440.Peer-Reviewed Original ResearchConceptsTranscription of PhoPPhoQ proteinDistinct binding sitesTwo-component regulatory systemGram-negative bacterium Salmonella typhimuriumPhoP/PhoQSingle amino acid substitutionBacterium Salmonella typhimuriumTryptophan intrinsic fluorescenceBinding sitesAmino acid substitutionsPeriplasmic domainAcid polypeptide
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
1995
Relationship between evolutionary rate and cellular location among the Inv/Spa invasion proteins of Salmonella enterica.
Li J, Ochman H, Groisman EA, Boyd EF, Solomon F, Nelson K, Selander RK. Relationship between evolutionary rate and cellular location among the Inv/Spa invasion proteins of Salmonella enterica. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 7252-7256. PMID: 7638176, PMCID: PMC41317, DOI: 10.1073/pnas.92.16.7252.Peer-Reviewed Original ResearchConceptsEvolutionary ratesInvasion genesInvasion proteinsCellular locationSequence identityProtein export systemNonphagocytic host cellsWarm-blooded vertebratesEnteric pathogens ShigellaSalmonella entericaS. entericaEvolutionary diversificationNiche expansionExport systemExtracellular environmentHost cellsSPA complexGenesEnteric bacteriaProteinFlagellar phaseKey eventsSubspeciesHomologuesSpa gene
1994
How bacteria resist killing by host-defense peptides
Groisman E. How bacteria resist killing by host-defense peptides. Trends In Microbiology 1994, 2: 444-449. PMID: 7866702, DOI: 10.1016/0966-842x(94)90802-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnti-Bacterial AgentsBacteriaDrug Resistance, MicrobialImmunity, InnateMolecular Sequence DataPeptidesVirulence