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
Analysis 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
1993
Analysis of the structure and subcellular location of filamentous phage pIV
Russel M, Kaźmierczak B. Analysis of the structure and subcellular location of filamentous phage pIV. Journal Of Bacteriology 1993, 175: 3998-4007. PMID: 8320216, PMCID: PMC204828, DOI: 10.1128/jb.175.13.3998-4007.1993.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseBacterial ProteinsCell CompartmentationColiphagesDNA Mutational AnalysisGene Expression Regulation, BacterialGenes, ViralHeat-Shock ProteinsMembrane ProteinsMutationOperonRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidSpheroplastsSubcellular FractionsViral ProteinsVirus ReplicationConceptsMembrane localization domainIntegral membrane proteinsSubstrate-binding domainAmino-terminal halfCarboxy-terminal halfSeries of genesCell fractionation studiesCytoplasmic domainPhage assemblyDeletion mutantsMembrane proteinsSubcellular locationLocalization domainFusion proteinFractionation studiesFilamentous phagePhosphatase activityFilamentous bacteriophageAlkaline phosphatase activityMissense mutationsProteinAssemblyDomainMutantsGenes