2019
The expanded specificity and physiological role of a widespread N-degron recognin
Gao X, Yeom J, Groisman EA. The expanded specificity and physiological role of a widespread N-degron recognin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 18629-18637. PMID: 31451664, PMCID: PMC6744884, DOI: 10.1073/pnas.1821060116.Peer-Reviewed Original ResearchConceptsN-degron pathwayN-terminusLarge hydrophobic amino acidsPhysiological roleAmino acidsN-terminal methionineFourth amino acidHydrophobic amino acidsProtease ClpAPClp proteinsProtein homeostasisProteolytic systemIntact proteinProteinTerminusPathwayClpAPDegronAlarmoneStrong preferenceOrganellesBindsBacteriumHomeostasisProteaseActivator of one protease transforms into inhibitor of another in response to nutritional signals
Yeom J, Groisman EA. Activator of one protease transforms into inhibitor of another in response to nutritional signals. Genes & Development 2019, 33: 1280-1292. PMID: 31371438, PMCID: PMC6719616, DOI: 10.1101/gad.325241.119.Peer-Reviewed Original ResearchConceptsNutritional signalsProtease specificityClpAP proteaseProtease LonProtein homeostasisParticular proteinToxic proteinsRegulatory roleParticular substrateRapid response mechanismProtein amountSpecific signalsResponse mechanismsProteaseProteinActivatorAcetylationProteomeCellsInhibitorsLonAdaptorSpecificityProteolysisBinds
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
2012
The promoter architectural landscape of the Salmonella PhoP regulon
Zwir I, Latifi T, Perez JC, Huang H, Groisman EA. The promoter architectural landscape of the Salmonella PhoP regulon. Molecular Microbiology 2012, 84: 463-485. PMID: 22435712, PMCID: PMC3335776, DOI: 10.1111/j.1365-2958.2012.08036.x.Peer-Reviewed Original ResearchConceptsPromoter architectureDistinct promoter architecturesPathogen Salmonella enterica serovar TyphimuriumGene expression behaviorSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumPhoP regulonPromoter featuresBiochemical functionsPhoPExpression behaviorPhysiological roleBacterial activatorsGenesSerovar TyphimuriumPromoterRegulonDifferent mechanismsTranscriptionVirulenceActivatorAncestryExpressionLarge numberLimited numberIntrinsic Negative Feedback Governs Activation Surge in Two-Component Regulatory Systems
Yeo WS, Zwir I, Huang HV, Shin D, Kato A, Groisman EA. Intrinsic Negative Feedback Governs Activation Surge in Two-Component Regulatory Systems. Molecular Cell 2012, 45: 409-421. PMID: 22325356, PMCID: PMC3713471, DOI: 10.1016/j.molcel.2011.12.027.Peer-Reviewed Original Research
2008
RstA-Promoted Expression of the Ferrous Iron Transporter FeoB under Iron-Replete Conditions Enhances Fur Activity in Salmonella enterica
Jeon J, Kim H, Yun J, Ryu S, Groisman EA, Shin D. RstA-Promoted Expression of the Ferrous Iron Transporter FeoB under Iron-Replete Conditions Enhances Fur Activity in Salmonella enterica. Journal Of Bacteriology 2008, 190: 7326-7334. PMID: 18790861, PMCID: PMC2576650, DOI: 10.1128/jb.00903-08.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBlotting, WesternElectrophoretic Mobility Shift AssayGene ExpressionGene Expression ProfilingGene Expression Regulation, BacterialIronIron DeficienciesOligonucleotide Array Sequence AnalysisOperonPromoter Regions, GeneticProtein BindingRepressor ProteinsReverse Transcriptase Polymerase Chain ReactionSalmonella entericaTranscription, GeneticConceptsFerrous iron transporter FeoBFur proteinIron-replete conditionsFur activityTarget genesIron-responsive genesWild-type levelsFerrous iron uptakeFeoAB operonFur geneTranscriptional activationIron acquisitionExpression experimentsRegulatory pathwaysTranscription levelsIron uptakeGenesPrimary regulatorRstAProteinFeOBRepressionSalmonella entericaPromoterExpressionOvercoming H-NS-mediated Transcriptional Silencing of Horizontally Acquired Genes by the PhoP and SlyA Proteins in Salmonella enterica *
Perez JC, Latifi T, Groisman EA. Overcoming H-NS-mediated Transcriptional Silencing of Horizontally Acquired Genes by the PhoP and SlyA Proteins in Salmonella enterica *. Journal Of Biological Chemistry 2008, 283: 10773-10783. PMID: 18270203, PMCID: PMC2447644, DOI: 10.1074/jbc.m709843200.Peer-Reviewed Original ResearchConceptsHistone-like nucleoid structuring proteinPagC geneSlyA proteinRNA polymeraseRNA polymerase recruitmentH-NS repressionNucleoid structuring proteinHorizontal gene transferDifferent regulatory proteinsSalmonella entericaPolymerase recruitmentTranscriptional silencingNew traitsForeign DNAGene transcriptionRegulatory proteinsUgtLRespective promotersTranscriptionPhoPRecipient organismGenesPagC promoterGene transferProtein
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 entericaVivoImmunoprecipitationMg2Transcriptional 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
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 questions
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 iron
1997
Regulation of polymyxin resistance and adaptation to low-Mg2+ environments
Groisman EA, Kayser J, Soncini FC. Regulation of polymyxin resistance and adaptation to low-Mg2+ environments. Journal Of Bacteriology 1997, 179: 7040-7045. PMID: 9371451, PMCID: PMC179645, DOI: 10.1128/jb.179.22.7040-7045.1997.Peer-Reviewed Original ResearchConceptsLPS modificationsAntimicrobial proteinsTranscription of PmrAPolymyxin resistanceWild-type organismsTwo-component systemExpression of pmrAAmino acid substitutionsPeptide antibiotic polymyxin BRegulatory proteinsPmrA-PmrBBacterial survivalAcid substitutionsMicromolar Mg2PmrAProteinHuman neutrophilsBacterial bindingGenesLociCationic polypeptidesAntibiotic polymyxin BOverall negative chargeSalmonella typhimuriumPhagocytic cells