2021
Cellular Adaptations to Cytoplasmic Mg2+ Limitation
Groisman EA, Chan C. Cellular Adaptations to Cytoplasmic Mg2+ Limitation. Annual Review Of Microbiology 2021, 75: 649-672. PMID: 34623895, DOI: 10.1146/annurev-micro-020518-115606.Peer-Reviewed Original ResearchConceptsCytoplasmic MgLeader regionATP-dependent proteaseTranscriptional regulator PhoPAbundant divalent cationOpen reading frameActivity of ribosomesSimilar adaptation strategiesRegulated proteolysisExpression of proteinsRegulator PhoPMicrobial speciesReading frameCellular adaptationDifferent genesCoding regionsBacterial speciesProtein synthesisSpeciesProteinAbundanceDivalent cationsExpressionCytoplasmic Mg2Enzymatic reactions
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 TyphimuriumGenesRho
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
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
The origin and evolution of species differences in Escherichia coli and Salmonella typhimurium
Ochman H, Groisman EA. The origin and evolution of species differences in Escherichia coli and Salmonella typhimurium. EXS 1994, 69: 479-493. PMID: 7994120, DOI: 10.1007/978-3-0348-7527-1_27.Peer-Reviewed Original ResearchConceptsSpecies-specific sequencesSalmonella chromosomeEscherichia coliCodon usage patternsOpen reading frameHost epithelial cellsCommon ancestorMap positionPhenotypic charactersReading frameBase compositionHorizontal transferSalmonella typhimuriumMutant strainGenetic differencesEnteric speciesBacterial speciesGenomePoint mutationsPhenotypic characteristicsSpeciesCorresponding regionChromosomesSpecies differencesEpithelial cells
1993
Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium.
Parra‐Lopez C, Baer MT, Groisman EA. Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium. The EMBO Journal 1993, 12: 4053-4062. PMID: 8223423, PMCID: PMC413698, DOI: 10.1002/j.1460-2075.1993.tb06089.x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAnti-Bacterial AgentsATP-Binding Cassette TransportersBase SequenceBiological TransportCloning, MolecularDrug Resistance, MicrobialEnterobacteriaceaeGenes, BacterialMelittenModels, BiologicalMolecular Sequence DataOperonPeptidesProtaminesSalmonella typhimuriumSequence Analysis, DNASequence Homology, Amino AcidConceptsUptake of oligopeptidesSet of genesOpen reading frameMolecular genetic analysisMammalian mdrYeast STE6Wild-type plasmidOperon structurePeriplasmic componentPeptide pheromoneNovel transporterReading frameKb segmentSalmonella typhimuriumGenetic analysisKb mRNASmall cationic peptidesSuccessful pathogenAntimicrobial peptide melittinSequence analysisCassette familyEnteric bacteriaPeptide transportAntimicrobial peptidesCancer cellsMolecular, functional, and evolutionary analysis of sequences specific to Salmonella.
Groisman EA, Sturmoski MA, Solomon FR, Lin R, Ochman H. Molecular, functional, and evolutionary analysis of sequences specific to Salmonella. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 1033-1037. PMID: 8430070, PMCID: PMC45805, DOI: 10.1073/pnas.90.3.1033.Peer-Reviewed Original ResearchConceptsAtypical base compositionIndependent evolutionary eventsPhenotypic characteristicsOpen reading frameLac gene fusionsWild-type parentLysR familyEvolutionary eventsDeletion strainEvolutionary analysisTranscriptional regulatorsReading frameSalmonella genomeNucleotide sequenceBase compositionHorizontal transferDNA fragmentsGene fusionsBacterial speciesEnteric bacteriaStructural similaritySpeciesVirulenceSequenceUnprecedented array