Beeby, M., Ferreira, J. L., Tripp, P., Albers, S. V. & Mitchell, D. R. Propulsive nanomachines: the convergent evolution of archaella, flagella and cilia. FEMS Microbiol. Rev. 44, 253–304 (2020).
Article CAS PubMed Google Scholar
Mondino, S., San Martin, F. & Buschiazzo, A. 3D cryo-EM imaging of bacterial flagella: novel structural and mechanistic insights into cell motility. J. Biol. Chem. 298, 102105 (2022).
Article CAS PubMed PubMed Central Google Scholar
Minamino, T. & Kinoshita, M. Structure, assembly, and function of flagella responsible for bacterial locomotion. EcoSal Plus 11, eesp00112023 (2023).
Zhou, J., Lloyd, S. A. & Blair, D. F. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl Acad. Sci. USA 95, 6436–6441 (1998).
Article CAS PubMed PubMed Central Google Scholar
Johnson, S. et al. Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation. Nat. Microbiol. 5, 966–975 (2020).
Article PubMed PubMed Central Google Scholar
Johnson, S. et al. Molecular structure of the intact bacterial flagellar basal body. Nat. Microbiol. 6, 712–721 (2021).
Article CAS PubMed PubMed Central Google Scholar
Johnson, S., Kuhlen, L., Deme, J. C., Abrusci, P. & Lea, S. M. The structure of an injectisome export gate demonstrates conservation of architecture in the core export gate between flagellar and virulence type III secretion systems. MBio 10, https://doi.org/10.1128/mBio.00818-19 (2019).
Kato, T., Makino, F., Miyata, T., Horvath, P. & Namba, K. Structure of the native supercoiled flagellar hook as a universal joint. Nat. Commun. 10, 5295 (2019).
Article PubMed PubMed Central Google Scholar
Kawamoto, A. et al. Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries. Nat. Commun. 12, 4223 (2021).
Article CAS PubMed PubMed Central Google Scholar
Singh, P. K., Cecchini, G., Nakagawa, T. & Iverson, T. M. CryoEM structure of a post-assembly MS-ring reveals plasticity in stoichiometry and conformation. PLoS ONE 18, e0285343 (2023).
Article CAS PubMed PubMed Central Google Scholar
Takekawa, N. et al. Two distinct conformations in 34 FliF subunits generate three different symmetries within the flagellar MS-ring. MBio 12, https://doi.org/10.1128/mBio.03199-20 (2021).
Tan, J. et al. Structural basis of assembly and torque transmission of the bacterial flagellar motor. Cell 184, 2665–2679 e2619 (2021).
Article CAS PubMed Google Scholar
Yamaguchi, T. et al. Structure of the molecular bushing of the bacterial flagellar motor. Nat. Commun. 12, 4469 (2021).
Article CAS PubMed PubMed Central Google Scholar
Thomas, D., Morgan, D. G. & DeRosier, D. J. Structures of bacterial flagellar motors from two FliF-FliG gene fusion mutants. J. Bacteriol. 183, 6404–6412 (2001).
Article CAS PubMed PubMed Central Google Scholar
Thomas, D. R., Francis, N. R., Xu, C. & DeRosier, D. J. The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium. J. Bacteriol. 188, 7039–7048 (2006).
Article CAS PubMed PubMed Central Google Scholar
Hess, J. F., Oosawa, K., Kaplan, N. & Simon, M. I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 53, 79–87 (1988).
Article CAS PubMed Google Scholar
Welch, M., Oosawa, K., Aizawa, S. & Eisenbach, M. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl Acad. Sci. USA 90, 8787–8791 (1993).
Article CAS PubMed PubMed Central Google Scholar
Cohen-Ben-Lulu, G. N. et al. The bacterial flagellar switch complex is getting more complex. EMBO J. 27, 1134–1144 (2008).
Article CAS PubMed PubMed Central Google Scholar
Koganitsky, A., Tworowski, D., Dadosh, T., Cecchini, G. & Eisenbach, M. A mechanism of modulating the direction of flagellar rotation in bacteria by fumarate and fumarate reductase. J. Mol. Biol. 431, 3662–3676 (2019).
Article CAS PubMed PubMed Central Google Scholar
Zarbiv, G. et al. Energy complexes are apparently associated with the switch-motor complex of bacterial flagella. J. Mol. Biol. 416, 192–207 (2012).
Article CAS PubMed Google Scholar
Zhang, H. et al. A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori. Mol. Microbiol. 106, 690–703 (2017).
Article CAS PubMed Google Scholar
Ko, M. & Park, C. Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli. J. Mol. Biol. 303, 371–382 (2000).
Article CAS PubMed Google Scholar
Fang, X. & Gomelsky, M. A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility. Mol. Microbiol. 76, 1295–1305 (2010).
Article CAS PubMed Google Scholar
Kaplan, M. et al. In situ imaging of the bacterial flagellar motor disassembly and assembly processes. EMBO J. 38, e100957 (2019).
Article PubMed PubMed Central Google Scholar
Kaplan, M. et al. Loss of the bacterial flagellar motor switch complex upon cell lysis. MBio 12, e0029821 (2021).
Johnson, S. et al. Structural basis of directonal switching by the bacterial flagellum. Preprint at Research Square, https://doi.org/10.21203/rs.3.rs-3417165/v1 (2023).
Lux, R., Kar, N. & Khan, S. Overproduced Salmonella typhimurium flagellar motor switch complexes. J. Mol. Biol. 298, 577–583 (2000).
Article CAS PubMed Google Scholar
Fernandez-Gimenez, E. et al. A new algorithm for particle weighted subtraction to decrease signals from unwanted components in single particle analysis. J. Struct. Biol. 215, 108024 (2023).
Article CAS PubMed Google Scholar
Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589 (2021).
Article CAS PubMed PubMed Central Google Scholar
Brown, P. N., Hill, C. P. & Blair, D. F. Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG. EMBO J. 21, 3225–3234 (2002).
Article CAS PubMed PubMed Central Google Scholar
Lam, K. H. et al. Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching. Structure 20, 315–325 (2012).
Article CAS PubMed Google Scholar
Lam, K. H. et al. Structural basis of FliG-FliM interaction in Helicobacter pylori. Mol. Microbiol. 88, 798–812 (2013).
Article CAS PubMed Google Scholar
Lloyd, S. A., Whitby, F. G., Blair, D. F. & Hill, C. P. Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor. Nature 400, 472–475 (1999).
Article CAS PubMed Google Scholar
Lynch, M. J. et al. Co-folding of a FliF-FliG split domain forms the basis of the MS:C ring interface within the bacterial flagellar motor. Structure 25, 317–328 (2017).
Article CAS PubMed PubMed Central Google Scholar
Minamino, T. et al. Structural insight into the rotational switching mechanism of the bacterial flagellar motor. PLoS Biol. 9, e1000616 (2011).
Article CAS PubMed PubMed Central Google Scholar
Xue, C. et al. Crystal structure of the FliF–FliG complex from Helicobacter pylori yields insight into the assembly of the motor MS-C ring in the bacterial flagellum. J. Biol. Chem. 293, 2066–2078 (2018).
Article CAS PubMed Google Scholar
Sircar, R. et al. Assembly states of FliM and FliG within the flagellar switch complex. J. Mol. Biol. 427, 867–886 (2015).
Article CAS PubMed Google Scholar
Lee, L. K., Ginsburg, M. A., Crovace, C., Donohoe, M. & Stock, D. Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching. Nature 466, 996–1000 (2010).
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