2024
Bacterial flagella hijack type IV pili proteins to control motility
Liu X, Tachiyama S, Zhou X, Mathias R, Bonny S, Khan M, Xin Y, Roujeinikova A, Liu J, Ottemann K. Bacterial flagella hijack type IV pili proteins to control motility. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2317452121. PMID: 38236729, PMCID: PMC10823254, DOI: 10.1073/pnas.2317452121.Peer-Reviewed Original Research
2022
A Tripartite Efflux System Affects Flagellum Stability in Helicobacter pylori
Gibson K, Chu JK, Zhu S, Nguyen D, Mrázek J, Liu J, Hoover TR. A Tripartite Efflux System Affects Flagellum Stability in Helicobacter pylori. International Journal Of Molecular Sciences 2022, 23: 11609. PMID: 36232924, PMCID: PMC9570263, DOI: 10.3390/ijms231911609.Peer-Reviewed Original ResearchConceptsTripartite efflux systemEfflux systemPeriplasmic membrane fusion proteinOuter membrane efflux proteinCryo-electron tomography studiesMembrane efflux proteinMembrane fusion proteinNumber of flagellaTransmembrane domainABC transportersUnsheathed flagellaSwimming motilityCandidate proteinsFusion proteinEfflux proteinsSame frameshift mutationFlagellaEnhanced motilityMutantsFlagellar sheathFrameshift mutationProteinIndependent variantsHomologP ringIn situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts
Cai S, Wu Y, Guillén-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203769119. PMID: 35858323, PMCID: PMC9303930, DOI: 10.1073/pnas.2203769119.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCryo-focused ion beam millingMembrane contact sitesCryo-electron tomographyFull-length structureLipid transport proteinsRod-like densitiesLysosome contactBinding partnerGenetic approachesHydrophobic grooveTransport proteinsContact sitesVps13Lipid transportAlphaFold predictionsFull-length modelHeLa cellsMembrane contactSitu architectureAdjacent membranesVPS13CProteinStructural informationEndo/lysosomesFliL 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 ResearchConceptsFlagellar motorBacterial motilityCryo-electron tomographyStator complexFlagellar proteinsMutant cellsPeriplasmic flagellaActive conformationSitu structureFascinating questionsSupramolecular complexesMotilityComplexesMotBOptimal functionFliLFlagellaIon fluxProteinFunctionAssemblyRemodelingCellsConformationBorrelia
2021
Characterization of the Flagellar Collar Reveals Structural Plasticity Essential for Spirochete Motility
Chang Y, Xu H, Motaleb MA, Liu J. Characterization of the Flagellar Collar Reveals Structural Plasticity Essential for Spirochete Motility. MBio 2021, 12: e02494-21. PMID: 34809456, PMCID: PMC8609358, DOI: 10.1128/mbio.02494-21.Peer-Reviewed Original ResearchConceptsLyme disease spirochete Borrelia burgdorferiPeriplasmic flagellaSpirochete motilityCryo-electron tomographySpirochete Borrelia burgdorferiRemarkable structural plasticityComplex host environmentSerious human diseasesFlagellar assemblyCollar ComplexMultiprotein complexesFlagellar collarFlagellar motorDistinct functionsDistinct morphologiesRemarkable plasticityHuman diseasesBorrelia burgdorferiHost environmentFlagellaStructural plasticityRemarkable groupMotilityProteinHost connective tissue
2020
Molecular mechanism for rotational switching of the bacterial flagellar motor
Chang Y, Zhang K, Carroll BL, Zhao X, Charon NW, Norris SJ, Motaleb MA, Li C, Liu J. Molecular mechanism for rotational switching of the bacterial flagellar motor. Nature Structural & Molecular Biology 2020, 27: 1041-1047. PMID: 32895555, PMCID: PMC8129871, DOI: 10.1038/s41594-020-0497-2.Peer-Reviewed Original ResearchConceptsBacterial flagellar motorSwitch proteinFlagellar motorResponse regulator CheYRotational switchingProton motive forceSwitch complexMolecular mechanismsPhosphorylated formMajor remodelingConformational changesMotive forceModel systemProteinBorrelia burgdorferiCheY3CheYMutantsTorque generatorFLIMInteractsCheXCW rotationMechanismRemodelingEstablishing 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 sporesGTPaseCellsCytoskeletonMyxococcusPeptidoglycanProteinBacteriumAn asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete
Gibson KH, Trajtenberg F, Wunder EA, Brady MR, San Martin F, Mechaly A, Shang Z, Liu J, Picardeau M, Ko A, Buschiazzo A, Sindelar CV. An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete. ELife 2020, 9: e53672. PMID: 32157997, PMCID: PMC7065911, DOI: 10.7554/elife.53672.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyKey functional attributesNative flagellar filamentsHigh-resolution cryo-electron tomographyPeriplasmic spaceSheath proteinStructural basisFlagellar filamentsLeptospira spirochetesSpirochete bacteriaEntire cellFunctional attributesX-ray crystallographyImportant pathogenSupercoilingMotilityBacteriaFilamentsCell bodiesFlagellaSpirochetesProteinFlagellinDistinctive meansEndoflagella
2019
Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography
Wang C, Tu J, Liu J, Molineux IJ. Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography. Nature Microbiology 2019, 4: 1049-1056. PMID: 30886360, PMCID: PMC6533119, DOI: 10.1038/s41564-019-0403-z.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyOuter membraneInfection initiationCell surfaceBacterial cell envelopeSalmonella enterica serovar TyphimuriumGenome translocationGram-negative bacteriaEnterica serovar TyphimuriumTail needleCytoplasmic membraneSecond proteinExtracellular channelsCell envelopePhage P22Successful infectionCell cytoplasmSerovar TyphimuriumSuch virionsGenomeCytoplasmProteinO-antigenPhagesAssembles
2018
Visualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis
Qin Z, Hu B, Liu J. Visualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis. Methods In Molecular Biology 2018, 1729: 187-199. PMID: 29429093, DOI: 10.1007/978-1-4939-7577-8_17.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyChemoreceptor arraysCheW coupling proteinLarge macromolecular assembliesChemotaxis arraysSubtomogram analysisCheA kinaseBacterial chemoreceptorsCellular contextCoupling proteinMacromolecular assembliesChemotaxis signalingMolecular levelSitu structurePrecise architectureBacterial minicellsMinicellsUnique toolKinaseSignalingProteinSubtomogramsAssemblyConcertAmplification
2008
The 3D Structure of Villin as an Unusual F-Actin Crosslinker
Hampton CM, Liu J, Taylor DW, DeRosier DJ, Taylor KA. The 3D Structure of Villin as an Unusual F-Actin Crosslinker. Structure 2008, 16: 1882-1891. PMID: 19081064, PMCID: PMC2782859, DOI: 10.1016/j.str.2008.09.015.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBinding SitesChickensCross-Linking ReagentsImage Processing, Computer-AssistedImaging, Three-DimensionalIntestinesMicrofilament ProteinsModels, MolecularMolecular Sequence DataMolecular WeightMuscle, SkeletalProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRabbitsSequence Homology, Amino Acid