2022
Identification and Characterization of the Alternative σ28 Factor in Treponema denticola
Kurniyati K, Chang Y, Liu J, Li C. Identification and Characterization of the Alternative σ28 Factor in Treponema denticola. Journal Of Bacteriology 2022, 204: e00248-22. PMID: 36043861, PMCID: PMC9487585, DOI: 10.1128/jb.00248-22.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coliFlagellaFlagellinGene Expression Regulation, BacterialSigma FactorTranscription FactorsTreponema denticolaConceptsDependent promotersTranscription factorsSpirochete Treponema denticolaGene expressionOral spirochete Treponema denticolaCryo-electron tomography analysisFlagellin gene expressionExpression of flagellinSite-directed mutagenesisFlagellar regulationChemotaxis genesPeriplasmic flagellaRNA polymeraseFliABacterial motilityTranscriptional factorsLate promoterExternal flagellaLines of evidenceEscherichia coliPromoterT. denticolaBiochemical analysisEssential roleE. coliFliL ring enhances the function of periplasmic flagella
Guo S, Xu H, Chang Y, Motaleb MA, Liu J. FliL ring enhances the function of periplasmic flagella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2117245119. PMID: 35254893, PMCID: PMC8931381, DOI: 10.1073/pnas.2117245119.Peer-Reviewed Original ResearchMeSH KeywordsBacterial Physiological PhenomenaBacterial ProteinsBorrelia burgdorferiFlagellaGene Expression Regulation, BacterialMembrane ProteinsModels, BiologicalModels, MolecularMolecular Motor ProteinsPeriplasmConceptsFlagellar motorBacterial motilityCryo-electron tomographyStator complexFlagellar proteinsMutant cellsPeriplasmic flagellaActive conformationSitu structureFascinating questionsSupramolecular complexesMotilityComplexesMotBOptimal functionFliLFlagellaIon fluxProteinFunctionAssemblyRemodelingCellsConformationBorrelia
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 ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyFlagellaGene Expression ProfilingGene Expression Regulation, BacterialGenetic Complementation TestHumansLeptospiraLeptospirosisMonomeric GTP-Binding ProteinsMutationSpirochaetalesVirulenceConceptsWild-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
2019
Loss of a Cardiolipin Synthase in Helicobacter pylori G27 Blocks Flagellum Assembly
Chu JK, Zhu S, Herrera CM, Henderson JC, Liu J, Trent MS, Hoover TR. Loss of a Cardiolipin Synthase in Helicobacter pylori G27 Blocks Flagellum Assembly. Journal Of Bacteriology 2019, 201: 10.1128/jb.00372-19. PMID: 31427391, PMCID: PMC6779456, DOI: 10.1128/jb.00372-19.Peer-Reviewed Original ResearchMeSH KeywordsAllelesBacterial ProteinsFlagellaGene Expression Regulation, BacterialHelicobacter pyloriHumansMembrane ProteinsMutagenesisMutationTranscriptomeTransferases (Other Substituted Phosphate Groups)ConceptsFlagellum assemblyFlagellum biosynthesisCardiolipin synthaseFlagellar protein export apparatusCardiolipin levelsProtein export apparatusCryo-electron tomographyWild-type levelsAllelic exchange mutagenesisMS ringFlagellar genesExport apparatusCell polesP ringHost colonizationMature flagellumCell envelopeGenomic DNAMutantsProximal rodFlagellaBiosynthesisSequencing analysisFlgIBacterial pathogensIn Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography
Zhu S, Schniederberend M, Zhitnitsky D, Jain R, Galán JE, Kazmierczak BI, Liu J. In Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography. Journal Of Bacteriology 2019, 201: 10.1128/jb.00117-19. PMID: 31010901, PMCID: PMC6560136, DOI: 10.1128/jb.00117-19.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyFlagellaGene Expression Regulation, BacterialPseudomonas aeruginosaSalmonella typhimuriumConceptsCryo-electron tomographyBacterial flagellaFlagellar assemblyPolar flagellumPeritrichous flagellaSerovar TyphimuriumSpecies-specific featuresBacterial pathogensOuter membrane complexSelf-assembling nanomachineFlagellar systemFlagellar structureFlagellar numberSubtomogram averagingMembrane complexLateral flagellaStructural basisDistinct flagellaMolecular machinesFlagellaSitu structureModel systemPseudomonasTyphimuriumRange of variation
2018
The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum
Zhu S, Nishikino T, Kojima S, Homma M, Liu J. The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum. Journal Of Bacteriology 2018, 200: 10.1128/jb.00387-18. PMID: 30104237, PMCID: PMC6182240, DOI: 10.1128/jb.00387-18.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyFlagellaGene DeletionGene Expression Regulation, BacterialPeriplasmVibrio alginolyticusConceptsPolar sheathed flagellumPeriplasmic flagellaExternal flagellaOuter membraneSheathed flagellumBacterial life cycleCryo-electron tomographyWild-type cellsInternal periplasmic flagellaMultiple peritrichous flagellaRemarkable nanomachinesFlagellar genesPeritrichous flagellaPeriplasmic spaceMost bacteriaNovel functionMolecular basisBacterial flagellaMajor organellesBacterial speciesFlagellaMembrane penetrationH-ringGenesLife cycleA unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel
Chetrit D, Hu B, Christie PJ, Roy CR, Liu J. A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel. Nature Microbiology 2018, 3: 678-686. PMID: 29784975, PMCID: PMC5970066, DOI: 10.1038/s41564-018-0165-z.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAnimalsBacterial ProteinsCryoelectron MicroscopyCytoplasmGene Expression Regulation, BacterialLegionella pneumophilaMiceModels, MolecularProtein MultimerizationRAW 264.7 CellsType IV Secretion SystemsConceptsCytoplasmic complexType IV secretion channelType IV secretion systemInner membrane complexTranslocation of substratesCryo-electron tomographySecretion channelCell polesCytoplasmic ATPaseSecretion systemT4SS functionHexameric assemblyMembrane complexCytoplasmic channelsDNA complexesSubstrate transferT4SSChannel activationATPaseComplexesDistinct stagesAssemblyBiogenesisATPasesFurther analysis