2012
The GTPase Activity of FlhF Is Dispensable for Flagellar Localization, but Not Motility, in Pseudomonas aeruginosa
Schniederberend M, Abdurachim K, Murray TS, Kazmierczak BI. The GTPase Activity of FlhF Is Dispensable for Flagellar Localization, but Not Motility, in Pseudomonas aeruginosa. Journal Of Bacteriology 2012, 195: 1051-1060. PMID: 23264582, PMCID: PMC3571332, DOI: 10.1128/jb.02013-12.Peer-Reviewed Original ResearchConceptsFlagellar functionGTPase activityOpportunistic human pathogen Pseudomonas aeruginosaHuman pathogen Pseudomonas aeruginosaSignal recognition particlePathogen Pseudomonas aeruginosaSingle-cell assaysFlhF proteinFlagellar localizationFlagellar assemblyRecognition particleAbiotic environmentProtein dimerizationFlagellar rotationNucleotide bindingFlhFPoint mutantsSurface organellesSwimming motilityBacterial motilityP. aeruginosaBacillus subtilisPseudomonas aeruginosaEnzymatic activityHydrolytic activity
2006
Mutational Analysis of RetS, an Unusual Sensor Kinase-Response Regulator Hybrid Required for Pseudomonas aeruginosa Virulence
Laskowski MA, Kazmierczak BI. Mutational Analysis of RetS, an Unusual Sensor Kinase-Response Regulator Hybrid Required for Pseudomonas aeruginosa Virulence. Infection And Immunity 2006, 74: 4462-4473. PMID: 16861632, PMCID: PMC1539586, DOI: 10.1128/iai.00575-06.Peer-Reviewed Original ResearchConceptsType III secretion system proteinsSignal transduction domainsSecretion system proteinsUpregulation of genesPeriplasmic domainSensor kinaseReceiver domainTransmembrane domainRegulator proteinTransduction domainMutational analysisSignaling roleSystem proteinsReciprocal regulationPseudomonas aeruginosaRET activityBiofilm formationVirulence factorsOpportunistic pathogenT3SSProteinRET alleleRETP. aeruginosaKey roleAnalysis 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
2001
Pseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair
Geiser T, Kazmierczak B, Garrity‐Ryan L, Matthay M, Engel J. Pseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair. Cellular Microbiology 2001, 3: 223-236. PMID: 11298646, DOI: 10.1046/j.1462-5822.2001.00107.x.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsEpithelial wound repairPseudomonas aeruginosa ExoTRho family GTPasesWound repairPathogen Pseudomonas aeruginosaNosocomial pathogen Pseudomonas aeruginosaP. aeruginosa internalizationEpithelial cellsP. aeruginosaGAP domainGAP activityBacterial proteinsCell roundingCytoskeleton collapseLung epithelial wound repairExoTCell detachmentVivo virulenceProteinEpithelial tissue damageImmune effector cellsLocal host defenseIntact epithelial barrierHost defense