2025
Identification of a Coxiella burnetii outer membrane porin required for intracellular replication
Yang Z, Duncan-Lowey J, Roy C. Identification of a Coxiella burnetii outer membrane porin required for intracellular replication. Infection And Immunity 2025, 93: e00448-24. PMID: 40071978, PMCID: PMC11977307, DOI: 10.1128/iai.00448-24.Peer-Reviewed Original ResearchConceptsIntracellular replicationDot/Icm type IVB secretion systemType IVB secretion systemHost cellsIsogenic wild-type strainIntracellular replication defectsIVB secretion systemEpitope-tagged proteinsOuter membrane porinsTransposon mutagenesis screenWild-type strainEpitope-tagged versionHost cell functionsBacterial outer membraneSecretion systemMembrane porinsMutagenesis screenOuter membraneReplication defectsHuman Q feverBacterial porinsMutantsGram-negativeIntracellular pathogensPorin
2021
Role of the major determinant of polar flagellation FlhG in the endoflagella‐containing spirochete Leptospira
Fule L, Halifa R, Fontana C, Sismeiro O, Legendre R, Varet H, Coppée J, Murray GL, Adler B, Hendrixson DR, Buschiazzo A, Guo S, Liu J, Picardeau M. Role of the major determinant of polar flagellation FlhG in the endoflagella‐containing spirochete Leptospira. Molecular Microbiology 2021, 116: 1392-1406. PMID: 34657338, DOI: 10.1111/mmi.14831.Peer-Reviewed Original ResearchConceptsWild-type strainSaprophyte L. biflexaCross-species complementationComparative transcriptome analysisPathogen L. interrogansFlagellar basal bodyCryo-electron tomographySpirochete LeptospiraSpiral-shaped morphologyFlagellar genesFlhGNumerical regulationTranscriptome analysisPeriplasmic flagellaFlhFCell motilityNegative regulatorBasal bodiesBacterial speciesL. biflexaMutantsGel-like environmentL. interrogansFlagellaBacteria
2015
Iron-dependent gene expression in Actinomyces oris
Mulé M, Giacalone D, Lawlor K, Golden A, Cook C, Lott T, Aksten E, O'Toole G, Bergeron L. Iron-dependent gene expression in Actinomyces oris. Journal Of Oral Microbiology 2015, 7: 29800. PMID: 26685151, PMCID: PMC4684579, DOI: 10.3402/jom.v7.29800.Peer-Reviewed Original ResearchIron-dependent gene expressionClinical isolatesA. orisGene expressionGrowth defectDegree of sequence similarityIron metabolismIron-replete mediumWild-type strainIsolates of ActinomycesHuman oral cavityIron-limiting conditionsIron-regulated genesIron-limited mediumIron transport systemGram-positive bacteriumIron-binding moleculesOral diseasesOral cavityDisease sitesActinomyces sppOral microbesComplemented strainsSequence similarityHigh-iron environment
2013
Engineering Geobacter sulfurreducens to produce a highly cohesive conductive matrix with enhanced capacity for current production
Leang C, Malvankar N, Franks A, Nevin K, Lovley D. Engineering Geobacter sulfurreducens to produce a highly cohesive conductive matrix with enhanced capacity for current production. Energy & Environmental Science 2013, 6: 1901-1908. DOI: 10.1039/c3ee40441b.Peer-Reviewed Original ResearchWild-type strainG. sulfurreducens genomeGeobacter sulfurreducensWild-type biofilmsCurrent-producing biofilmsSimple genetic manipulationProduction of piliPilZ domainGenetic manipulationStrain CL-1Charge transfer resistanceCL-1Conductive matrixMicrobial fuel cellsConductive biofilmsBioelectronic materialsPotential applicationsEnergy applicationsBiofilmsGreater conductivityBiofilm productionGraphite electrodeTransfer resistanceBiofilm propertiesSulfurreducens
2008
Targeted Mutagenesis in Pathogenic Leptospira Species: Disruption of the LigB Gene Does Not Affect Virulence in Animal Models of Leptospirosis
Croda J, Figueira CP, Wunder EA, Santos CS, Reis MG, Ko AI, Picardeau M. Targeted Mutagenesis in Pathogenic Leptospira Species: Disruption of the LigB Gene Does Not Affect Virulence in Animal Models of Leptospirosis. Infection And Immunity 2008, 76: 5826-5833. PMID: 18809657, PMCID: PMC2583567, DOI: 10.1128/iai.00989-08.Peer-Reviewed Original ResearchConceptsPathogenic Leptospira speciesLeptospira speciesAcute disease manifestationsPersistent renal colonizationInoculation of ratsDisease manifestationsHamster modelRenal colonizationPathogenic mechanismsAnimal modelsPersistent colonizationDecrease virulenceLeptospira interrogansHomologous recombinationLeptospirosisVirulence factorsBacterial adherenceImmunoblot analysisCorresponding chromosomal locusWild-type strainCultured cellsFirst evidenceSpectinomycin resistance geneRepeat proteinsTargeted Mutagenesis
2006
Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
Nishino K, Hsu FF, Turk J, Cromie MJ, Wösten MM, Groisman EA. Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III). Molecular Microbiology 2006, 61: 645-654. PMID: 16803591, PMCID: PMC1618816, DOI: 10.1111/j.1365-2958.2006.05273.x.Peer-Reviewed Original ResearchMeSH KeywordsAluminumBacterial ProteinsBase SequenceDrug Resistance, BacterialEscherichia coli ProteinsGene Expression Regulation, BacterialIronLipid ALipopolysaccharidesMolecular Sequence DataMutationPeriplasmPhosphoric Monoester HydrolasesPhosphorylationPolymyxin BSalmonella typhimuriumSoil MicrobiologyTranscription FactorsConceptsPmrA/PmrB systemGram-negative bacterial speciesNon-host environmentsPmrA/PmrBWild-type strainSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumOuter membraneLipopolysaccharide modificationBacterial speciesCovalent modificationResistance genesSerovar TyphimuriumOxygen-dependent killingPmrAEssential metalsHomeostatic mechanismsSalmonella survivalMutantsDephosphorylationGenesSpeciesProteinMajor constituentsIdentificationAnalysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
Kazmierczak BI, Lebron MB, Murray TS. Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Molecular Microbiology 2006, 60: 1026-1043. PMID: 16677312, PMCID: PMC3609419, DOI: 10.1111/j.1365-2958.2006.05156.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell MovementCyclic GMPEscherichia coli ProteinsFemaleFimbriae, BacterialHeLa CellsHumansMiceMice, Inbred C57BLPhosphoric Diester HydrolasesPhosphorus-Oxygen LyasesPneumonia, BacterialPoint MutationProtein Structure, TertiaryPseudomonas aeruginosaSequence DeletionVirulenceConceptsEAL domainBacterial poleGGDEF-EAL proteinsCyclic dimeric guanosine monophosphateDiguanylate cyclase activityPolar surface structuresType IV piliWild-type strainGGDEF domainDiguanylate cyclasesREC domainLocalization signalPilus assemblyGGDEFNon-polar sitesFimXSurface piliPseudomonas aeruginosaPhosphodiesterase activityBiofilm formationProteinMutantsPiliMotilityDomain
2005
Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.
Kamińska J, Kwapisz M, Grabińska K, Orłowski J, Boguta M, Palamarczyk G, Zoładek T. Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae. Acta Biochimica Polonica 2005, 52: 207-20. PMID: 15827618, DOI: 10.18388/abp.2005_3510.Peer-Reviewed Original ResearchConceptsCell wall integrityIsoprenoid pathwayWall integrityPlasma membraneRsp5 ubiquitin-protein ligaseCell wallCell wall organizationRsp5 ubiquitin ligaseUbiquitin-protein ligaseCell wall structureWild-type strainNorthern blot analysisWall organizationProtein glycosylationDimethylallyl diphosphateType strainUbiquitin ligaseIsopentenyl diphosphateS. cerevisiaeCytosolic distributionErgosterol biosynthesisKey enzymeRegulatory roleChitin levelsMolecular level
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 entericaVivoImmunoprecipitationMg2
2002
Fe(III)‐mediated cellular toxicity
Chamnongpol S, Dodson W, Cromie MJ, Harris ZL, Groisman EA. Fe(III)‐mediated cellular toxicity. Molecular Microbiology 2002, 45: 711-719. PMID: 12139617, DOI: 10.1046/j.1365-2958.2002.03041.x.Peer-Reviewed Original ResearchConceptsIsogenic wild-type strainSignal transduction systemWild-type strainGram-negative speciesPmrA mutantOuter membraneIron-mediated toxicityTransduction systemMicrobicidal activityBacterial survivalMajor regulatorCell deathPmrA geneIron homeostasisMutantsEscherichia coliSalmonella mutantsDeleterious metalsCellular toxicitySalmonella entericaExcellent biocatalystAnaerobic conditionsGenesRegulatorSpecies
2000
The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri
Moss J, Fisher P, Vick B, Groisman E, Zychlinsky A. The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri. Cellular Microbiology 2000, 2: 443-452. PMID: 11207599, DOI: 10.1046/j.1462-5822.2000.00065.x.Peer-Reviewed Original ResearchConceptsWild-type strainPhoP mutantPhoP/PhoQ systemTwo-component regulatory systemRegulatory protein PhoPHost cell phagosomesPhoP/PhoQKey virulence genesMutant bacteriaEnteric bacteriumPathogen escapeCell phagosomesHost cellsMutantsWild-type ShigellaPolymorphonuclear leucocytesRegulatory systemVirulence genesAntimicrobial moleculesAntimicrobial peptidesPhoPExtreme acidInflammatory responseEpithelial cellsPhagosomes
1999
Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes
Sobel S, Wolin S. Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes. Molecular Biology Of The Cell 1999, 10: 3849-3862. PMID: 10564276, PMCID: PMC25684, DOI: 10.1091/mbc.10.11.3849.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensFungal ProteinsGene DeletionGene Expression Regulation, FungalMicrofilament ProteinsMolecular Sequence DataPhylogenyPolyribosomesProtein BiosynthesisProtein Synthesis InhibitorsRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentConceptsRNA-binding proteinLa proteinRNA polymerase III transcriptsMotif-containing proteinsSaccharomyces cerevisiae proteinsPolymerase III transcriptsWild-type strainCerevisiae proteinsLa motifProtein synthesis inhibitorU6 RNASro9pIndirect immunofluorescence microscopyMRNA translationImmunofluorescence microscopyLhp1pEssential processProteinSynthesis inhibitorNormal pathwayDeletionMotifLHP1SLF1Ribosomes
1998
YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF‐α production and downregulation of the MAP kinases p38 and JNK
Palmer L, Hobbie S, Galán J, Bliska J. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF‐α production and downregulation of the MAP kinases p38 and JNK. Molecular Microbiology 1998, 27: 953-965. PMID: 9535085, DOI: 10.1046/j.1365-2958.1998.00740.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial Outer Membrane ProteinsCalcium-Calmodulin-Dependent Protein KinasesCell LineCloning, MolecularDown-RegulationEnzyme ActivationGene Expression Regulation, BacterialGenetic Complementation TestImmunoblottingJNK Mitogen-Activated Protein KinasesLipopolysaccharidesMacrophagesMiceMitogen-Activated Protein KinasesMutationp38 Mitogen-Activated Protein KinasesTumor Necrosis Factor-alphaYersinia pseudotuberculosisConceptsY. pseudotuberculosisTNF-alpha productionMitogen-activated protein kinaseType III pathwayWild-type Y. pseudotuberculosisWild-type strainTNF-alphaPathogenic Yersinia sppYop genesYop proteinsYop secretionProtein kinaseMAP kinaseTranslational levelMutantsExposure of macrophagesYopJYersinia pseudotuberculosisSustained activationMacrophage TNF-α productionJNKP38Yersinia sppTumor necrosis factor alphaJ774A.1 murine macrophages
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 fusionIdentification 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 flagellin
1992
Molecular genetic analysis of the Escherichia coli phoP locus
Groisman EA, Heffron F, Solomon F. Molecular genetic analysis of the Escherichia coli phoP locus. Journal Of Bacteriology 1992, 174: 486-491. PMID: 1530848, PMCID: PMC205741, DOI: 10.1128/jb.174.2.486-491.1992.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceIsogenic wild-type strainE. coli genomePhoP geneMajor virulence regulatorAmino acid sequenceWild-type strainTwo-component systemMolecular genetic analysisColi genomePhoP locusVirulence regulatorIntramacrophage survivalAcid sequenceGenetic analysisEnteric speciesPhoP mutantE. coliGenesMagainin 2Cationic peptidesPhagocytic cellsGenomeHomologMutants
1989
A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes.
Willis I, Schmidt P, Söll D. A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes. The EMBO Journal 1989, 8: 4281-4288. PMID: 2686985, PMCID: PMC401634, DOI: 10.1002/j.1460-2075.1989.tb08614.x.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCloning, MolecularDNA-Directed RNA PolymerasesGene ExpressionGenes, DominantGenes, FungalKineticsMolecular Sequence DataMutationOligonucleotide ProbesPlasmidsPromoter Regions, GeneticRNA Polymerase IIIRNA, RibosomalRNA, Ribosomal, 5SRNA, TransferSaccharomyces cerevisiaeSaccharomycetalesSchizosaccharomycesSelection, GeneticSuppression, GeneticTemplates, GeneticTranscription, GeneticConceptsTRNA genesMutant strainTranscription of mutantsTranscription of tRNARNA polymerase IIISuppressor tRNA geneDominant mutant geneWild-type strainStable complexesTranscription apparatusRNA genesStable complex formationUpstream geneTRNA suppressorsPositive regulatorSteady-state levelsComplex assemblyGenetic approachesPolymerase IIIGene transcriptionInternal promoterMutant geneTime-course experimentsTranscriptionGenes
1988
Tyrosinases of murine melanocytes with mutations at the albino locus.
Halaban R, Moellmann G, Tamura A, Kwon BS, Kuklinska E, Pomerantz SH, Lerner AB. Tyrosinases of murine melanocytes with mutations at the albino locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7241-7245. PMID: 3140237, PMCID: PMC282161, DOI: 10.1073/pnas.85.19.7241.Peer-Reviewed Original ResearchConceptsAlbino locusTrans-Golgi networkWild-type melanocytesWild-type strainAbnormal posttranslational modificationsSynthesis of melaninDiminished pigmentationStructural genePosttranslational modificationsMurine melanocytesLocus mutantsKey enzymeLevels of mRNAMutantsKinetics of activationProteolytic cleavageUnstable enzymeEnzymeLociMelanocytesReduced levelsMutationsConfer susceptibilityTyrosinaseLittle enzyme
1981
Initiation of Aggregation by Dictyostelium discoideum in Mutant Populations Lacking Pulsatile Signalling
GLAZER P, NEWELL P. Initiation of Aggregation by Dictyostelium discoideum in Mutant Populations Lacking Pulsatile Signalling. Microbiology 1981, 125: 221-232. DOI: 10.1099/00221287-125-2-221.Peer-Reviewed Original ResearchDictyostelium discoideumAggregation centersCell surface cyclic AMP receptorsAggregation-deficient mutantsContact site AWild-type cellsCyclic AMP receptorsWild-type strainCyclic AMP signalsWild-type amoebaeWild-type populationAmoebal populationsCyclic AMP pulsesActive adenylate cyclaseAMP receptorsCyclic AMPAMP signalsMutantsAggregation signalsAMP pulsesInitiation of aggregationDiscoideumPulsatile regulationCell adhesiveMixed population
1980
Impaired incision of ultraviolet-irradiated deoxyribonucleic acid in uvrC mutants of Escherichia coli
Seeberg E, Rupp WD, Strike P. Impaired incision of ultraviolet-irradiated deoxyribonucleic acid in uvrC mutants of Escherichia coli. Journal Of Bacteriology 1980, 144: 97-104. PMID: 6998973, PMCID: PMC294597, DOI: 10.1128/jb.144.1.97-104.1980.Peer-Reviewed Original ResearchConceptsUvrC mutantsGene productsUvrA mutantStrand incisionUltraviolet-irradiated deoxyribonucleic acidEscherichia coli KWild-type strainExcision repair pathwayCell-free systemDeoxyribonucleic acidToluene-treated cellsDouble mutantSingle-strand breaksRepair pathwaysColi KMutantsBreak formationBreak accumulationEscherichia coliInhibitor nicotinamideStrand breakageVivoSlow accumulationAccumulationBreaks
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