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 preferenceOrganellesBindsBacteriumHomeostasisProtease
2018
Reduction in adaptor amounts establishes degradation hierarchy among protease substrates
Yeom J, Gao X, Groisman EA. Reduction in adaptor amounts establishes degradation hierarchy among protease substrates. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e4483-e4492. PMID: 29686082, PMCID: PMC5948988, DOI: 10.1073/pnas.1722246115.Peer-Reviewed Original ResearchConceptsRegulatory protein PhoPATP-dependent proteaseCritical cellular processesExpression of genesCellular processesAntibiotic persistersCytoplasmic MgProtease substratesUvrYDifferential stabilityProteasePhoPPhysiological conditionsGenesAdaptorAbundanceUnfoldaseFtsATranscriptionSubunitsSubstrateProteolysisVirulenceProteinBinds
2013
Bacterial Mg2+ Homeostasis, Transport, and Virulence
Groisman EA, Hollands K, Kriner MA, Lee EJ, Park SY, Pontes MH. Bacterial Mg2+ Homeostasis, Transport, and Virulence. Annual Review Of Genetics 2013, 47: 625-646. PMID: 24079267, PMCID: PMC4059682, DOI: 10.1146/annurev-genet-051313-051025.Peer-Reviewed Original Research
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 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 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
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
1994
A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium.
Parra‐Lopez C, Lin R, Aspedon A, Groisman EA. A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium. The EMBO Journal 1994, 13: 3964-3972. PMID: 8076592, PMCID: PMC395316, DOI: 10.1002/j.1460-2075.1994.tb06712.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBiological TransportCarrier ProteinsCloning, MolecularDrug Resistance, MicrobialMelittenMembrane ProteinsMolecular Sequence DataNADPeptidesPotassiumProtaminesReceptor, trkARecombinant ProteinsRestriction MappingSalmonella typhimuriumSequence Analysis, DNASequence Homology, Amino AcidConceptsE. coli proteinsAntimicrobial peptidesMolecular genetic analysisAntimicrobial peptide protaminePutative transportersTransport of peptidesColi proteinsSingle mutantsSalmonella proteinsSame resistance pathwaysSAP mutantsHost defense moleculesGenetic analysisDefense moleculesLoci participateChannel proteinsExhibit hypersensitivityEfflux proteinsUptake systemResistance pathwaysMutantsEscherichia coliProteinTransport of potassiumHost tissues
1991
Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein
Vartak NB, Reizer J, Reizer A, Gripp JT, Groisman EA, Wu L, Tomich JM, Saier MH. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Research In Microbiology 1991, 142: 951-963. PMID: 1805309, DOI: 10.1016/0923-2508(91)90005-u.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCarrier ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsFructoseGene Expression Regulation, BacterialIn Vitro TechniquesOperator Regions, GeneticOperonPeriplasmic Binding ProteinsPromoter Regions, GeneticRepressor ProteinsRestriction MappingSalmonella typhimuriumConceptsRibose binding proteinTranscriptional regulatory proteinsN-terminal hydrophobic signal sequenceRegulatory proteinsPeriplasmic ribose-binding proteinBacterial DNA-binding proteinsHydrophobic signal sequencePeriplasmic binding proteinRibose-binding proteinDNA-binding proteinsCentral metabolic pathwaysN-terminal regionOperator-promoter regionChemoreception systemFructose operonSignature motifTranscriptional regulationRepressor functionHelix motifPhylogenetic treeSignal sequenceGene sequencesNucleotide sequenceSequence identitySalmonella typhimurium