Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi

Periplasmic flagella are essential for the distinctive morphology, motility, and infectious life cycle of the Lyme disease spirochete Borrelia burgdorferi . In this study, we genetically trapped intermediates in flagellar assembly and determined the 3D structures of the intermediates to 4-nm resolut...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 110; no. 35; pp. 14390 - 14395
Main Authors Zhao, Xiaowei, Zhang, Kai, Boquoi, Tristan, Hu, Bo, Motaleb, M. A., Miller, Kelly A., James, Milinda E., Charon, Nyles W., Manson, Michael D., Norris, Steven J., Li, Chunhao, Liu, Jun
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 27.08.2013
National Acad Sciences
Subjects
Architecture
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biological Sciences
Borrelia burgdorferi
Borrelia burgdorferi - genetics
Borrelia burgdorferi - metabolism
Cells
Electrons
Flagella
Flagella - metabolism
Lyme disease
Morphology
Motors
Mutation
Protein Conformation
Salmonella typhimurium
Secretion
Spirochaetales
Stators
Tomography
Tomography - methods
bacterial motility
molecular machines
protein secretion
macromolecular assemblages
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Summary:Periplasmic flagella are essential for the distinctive morphology, motility, and infectious life cycle of the Lyme disease spirochete Borrelia burgdorferi . In this study, we genetically trapped intermediates in flagellar assembly and determined the 3D structures of the intermediates to 4-nm resolution by cryoelectron tomography. We provide structural evidence that secretion of rod substrates triggers remodeling of the central channel in the flagellar secretion apparatus from a closed to an open conformation. This open channel then serves as both a gateway and a template for flagellar rod assembly. The individual proteins assemble sequentially to form a modular rod. The hook cap initiates hook assembly on completion of the rod, and the filament cap facilitates filament assembly after formation of the mature hook. Cryoelectron tomography and mutational analysis thus combine synergistically to provide a unique structural blueprint of the assembly process of this intricate molecular machine in intact cells.
Bibliography:http://dx.doi.org/10.1073/pnas.1308306110
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Edited by David DeRosier, Brandeis University, Waltham, MA, and approved July 12, 2013 (received for review May 2, 2013)
1X.Z. and K.Z. contributed equally to this work.
Author contributions: C.L. and J.L. designed research; X.Z., K.Z., T.B., B.H., M.A.M., K.A.M., M.E.J., N.W.C., C.L., and J.L. performed research; K.Z., M.A.M., C.L., and J.L. contributed new reagents/analytic tools; X.Z., K.Z., M.A.M., M.D.M., S.J.N., C.L., and J.L. analyzed data; and X.Z., M.A.M., M.D.M., S.J.N., C.L., and J.L. wrote the paper.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1308306110