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Bacterial flagellar motor PL-ring disassembly Sub-complexes are widespread and ancient

Mohammed Kaplan, Michael J. Sweredoski, View ORCID ProfileJoão P.G.L.M. Rodrigues, Elitza I. Tocheva, Yi-Wei Chang, Davi R. Ortega, Morgan Beeby, Grant J. Jensen
doi: https://doi.org/10.1101/786715
Mohammed Kaplan
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
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Michael J. Sweredoski
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
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João P.G.L.M. Rodrigues
2Department of Structural Biology, Stanford University, Stanford, CA, USA
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  • ORCID record for João P.G.L.M. Rodrigues
Elitza I. Tocheva
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
3Department of Microbiology and Immunology, Life Sciences Institute, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada
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Yi-Wei Chang
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
4Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
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Davi R. Ortega
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
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Morgan Beeby
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
5Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK
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Grant J. Jensen
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
6Howard Hughes Medical Institute, 1200 E. California Boulevard, Pasadena, CA 91125, USA
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  • For correspondence: Jensen@caltech.edu
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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 decorated 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.

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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.
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Posted September 30, 2019.
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Bacterial flagellar motor PL-ring disassembly Sub-complexes are widespread and ancient
Mohammed Kaplan, Michael J. Sweredoski, João P.G.L.M. Rodrigues, Elitza I. Tocheva, Yi-Wei Chang, Davi R. Ortega, Morgan Beeby, Grant J. Jensen
bioRxiv 786715; doi: https://doi.org/10.1101/786715
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Bacterial flagellar motor PL-ring disassembly Sub-complexes are widespread and ancient
Mohammed Kaplan, Michael J. Sweredoski, João P.G.L.M. Rodrigues, Elitza I. Tocheva, Yi-Wei Chang, Davi R. Ortega, Morgan Beeby, Grant J. Jensen
bioRxiv 786715; doi: https://doi.org/10.1101/786715

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