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
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
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 signalsProteinExpressionPhoPMgtAEvolution of a Bacterial Regulon Controlling Virulence and Mg2+ Homeostasis
Perez JC, Shin D, Zwir I, Latifi T, Hadley TJ, Groisman EA. Evolution of a Bacterial Regulon Controlling Virulence and Mg2+ Homeostasis. PLOS Genetics 2009, 5: e1000428. PMID: 19300486, PMCID: PMC2650801, DOI: 10.1371/journal.pgen.1000428.Peer-Reviewed Original ResearchConceptsRegulatory proteinsSpecies-specific traitsHorizontal gene transferDifferent gene setsSpecies-specific targetsPhoP proteinTranscriptional rewiringPhoP regulonRelated organismsPhoPQ operonGene setsVariable membersCell envelopeProtein activityRegulonBacterial speciesGene transferSpeciesProteinPhoPFamily EnterobacteriaceaeGenesVirulenceHomeostasisWidespread effects
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
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 macrophagesMutantsEndosomesGenes
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
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 cells