Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 13, Pages E1917-E1926Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1518952113
Keywords
bacterial flagellar motors; electron cryo-tomography; macromolecular evolution; torque; Campylobacter
Categories
Funding
- Biotechnology and Biological Sciences Research Council [BB/L023091/1]
- Howard Hughes Medical Institute
- National Institutes of Health [5R01AI065539, 5R21AI103643]
- Biotechnology and Biological Sciences Research Council [BB/L023091/1] Funding Source: researchfish
- BBSRC [BB/L023091/1] Funding Source: UKRI
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Although it is known that diverse bacterial flagellar motors produce different torques, the mechanism underlying torque variation is unknown. To understand this difference better, we combined genetic analyses with electron cryo-tomography subtomogram averaging to determine in situ structures of flagellar motors that produce different torques, from Campylobacter and Vibrio species. For the first time, to our knowledge, our results unambiguously locate the torque-generating stator complexes and show that diverse high-torque motors use variants of an ancestrally related family of structures to scaffold incorporation of additional stator complexes at wider radii from the axial driveshaft than in the model enteric motor. We identify the protein components of these additional scaffold structures and elucidate their sequential assembly, demonstrating that they are required for stator-complex incorporation. These proteins are widespread, suggesting that different bacteria have tailored torques to specific environments by scaffolding alternative stator placement and number. Our results quantitatively account for different motor torques, complete the assignment of the locations of the major flagellar components, and provide crucial constraints for understanding mechanisms of torque generation and the evolution of multiprotein complexes.
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