2020
Establishing rod shape from spherical, peptidoglycan-deficient bacterial spores
Zhang H, Mulholland GA, Seef S, Zhu S, Liu J, Mignot T, Nan B. Establishing rod shape from spherical, peptidoglycan-deficient bacterial spores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 14444-14452. PMID: 32513721, PMCID: PMC7321990, DOI: 10.1073/pnas.2001384117.Peer-Reviewed Original ResearchConceptsBacterial actin homolog MreBFuture cell polesActin homolog MreBGTPase-activating proteinsMolecular motorsGram-negative bacteriumCell polesEukaryotic cellsSynthesis complexSpherical sporesWalled cellsRod shapeMglBMglAPG growthSporesMreBBacterial sporesGTPaseCellsCytoskeletonMyxococcusPeptidoglycanProteinBacteriumFlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi
Zhang K, He J, Catalano C, Guo Y, Liu J, Li C. FlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi. Molecular Microbiology 2020, 113: 1122-1139. PMID: 32039533, PMCID: PMC8085991, DOI: 10.1111/mmi.14482.Peer-Reviewed Original ResearchConceptsPeriplasmic flagellaCell polesM-ring proteinLyme disease bacterium Borrelia burgdorferiCryo-electron tomography studiesSignal recognition particlePolar localizationB. burgdorferiFlagellar assemblyRecognition particleMutant cellsFlagellar numberProtein stabilityFlagellar patternBorrelia burgdorferiFlhFEnzymatic activityBiochemical analysisMechanistic insightsBacterium Borrelia burgdorferiFlagellaPF numberBacteriaMidcellDetailed characterizationAnalysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding
Park D, Chetrit D, Hu B, Roy CR, Liu J. Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding. MBio 2020, 11: 10.1128/mbio.03328-19. PMID: 32071271, PMCID: PMC7029142, DOI: 10.1128/mbio.03328-19.Peer-Reviewed Original ResearchConceptsType IV secretion systemSecretion systemCryoelectron tomographyInner membraneDot/Icm apparatusConformational changesDot/IcmEukaryotic host cellsBacterial inner membraneWild-type cellsHost cell membraneWhole-cell contextMultiprotein nanomachineSubtomogram analysisSophisticated nanomachinesCytoplasmic substratesProtein effectorsCell polesDNA substratesSubtomogram averagingATPase complexDNA transferHost infectionStructural basisHost cells
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 ResearchConceptsFlagellum 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 pathogens
2018
A 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 ResearchConceptsCytoplasmic 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