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Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export

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  • Tohru Minamino

    (Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
    Dynamic NanoMachine Project, ICORP, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Keiichi Namba

    (Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
    Dynamic NanoMachine Project, ICORP, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan)

Abstract

Alternative energy Bacterial flagella contain a secretion apparatus related to the type III secretion system used by many pathogens to transfer effector proteins into host cells. It is generally assumed that the ATPase FliI provides energy for transport, but two reports argue against this view. Both groups find that flagellar secretion occurs even in the absence of the ATPase, and that the energy required derives from the proton motive force.

Suggested Citation

  • Tohru Minamino & Keiichi Namba, 2008. "Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export," Nature, Nature, vol. 451(7177), pages 485-488, January.
    • Handle: RePEc:nat:nature:v:451:y:2008:i:7177:d:10.1038_nature06449
    DOI: 10.1038/nature06449
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    Cited by:

    1. Imke Spöring & Vincent A Martinez & Christian Hotz & Jana Schwarz-Linek & Keara L Grady & Josué M Nava-Sedeño & Teun Vissers & Hanna M Singer & Manfred Rohde & Carole Bourquin & Haralampos Hatzikirou , 2018. "Hook length of the bacterial flagellum is optimized for maximal stability of the flagellar bundle," PLOS Biology, Public Library of Science, vol. 16(9), pages 1-19, September.

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