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Published October 2, 2019 | Submitted
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Bacterial flagellar motor PL-ring disassembly sub-complexes are widespread and ancient

Abstract

The bacterial flagellar motor is an amazing nanomachine. Understanding how such complex structures arose is crucial to our understanding of cellular evolution. We and others recently reported that in several Gammaproteobacterial species, a relic sub-complex comprising the P- and L-rings persists in the outer membrane after flagellum disassembly. Imaging nine additional species with cryo-electron tomography, here we show that this sub-complex persists after flagellum disassembly in other phyla as well. Bioinformatic analyses fail to show evidence of any recent horizontal transfers of the P- and L-ring genes, suggesting that this sub-complex and its persistence is an ancient and conserved feature of the flagellar motor. We hypothesize that one function of the P- and L-rings is to seal the outer membrane after motor disassembly.

Additional Information

The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license. This work was supported by NIH grant R35 GM122588 to GJJ. Cryo-EM work was done in the Beckman Institute Resource Center for Transmission Electron Microscopy at Caltech. M.K. acknowledges a Rubicon postdoctoral fellowship from De Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO). Ariane Briegel kindly helped in collecting part of the data. We thank Catherine M. Oikonomou for reading the manuscript and for the insightful discussions. We thank Dr. Pat Zambryski from the University of California, Berkeley for providing us with A. longum strain used in this study.

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August 19, 2023
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