FusB energizes import across the outer membrane through direct interaction with its ferredoxin substrate

Wojnowska, Marta and Walker, Daniel (2020) FusB energizes import across the outer membrane through direct interaction with its ferredoxin substrate. mBio, 11 (5). pp. 1-11. ISSN 2150-7511 (https://doi.org/10.1128/mBio.02081-20)

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Abstract

Phytopathogenic Pectobacterium spp. import ferredoxin into the periplasm for proteolytic processing and iron release via the ferredoxin uptake system. Although the ferredoxin receptor FusA and the processing protease FusC have been identified, the mechanistic basis of ferredoxin import is poorly understood. In this work, we demonstrate that protein translocation across the outer membrane is dependent on the TonB-like protein FusB. In contrast to the loss of FusC, loss of FusB or FusA abolishes ferredoxin transport to the periplasm, demonstrating that FusA and FusB work in concert to transport ferredoxin across the outer membrane. In addition to an interaction with the “TonB box” region of FusA, FusB also forms a complex with the ferredoxin substrate, with complex formation required for substrate transport. These data suggest that ferredoxin transport requires energy transduction from the cytoplasmic membrane via FusB both for removal of the FusA plug domain and for substrate translocation through the FusA barrel.

  • Item type:Article
    ID code:86295
    Dates:
    Date
    Event
    27 October 2020
    Published
    5 October 2020
    Accepted
    24 July 2020
    Submitted
    Notes:© 2020 Wojnowska and Walker. Wojnowska M, Walker D. 2020. FusB energizes import across the outer membrane through direct interaction with its ferredoxin substrate. mBio 11:e02081-20. https://doi.org/10.1128/mBio.02081-20
    Subjects:Science > Microbiology
    Department:Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
    Depositing user: Pure Administrator
    Date deposited:27 Jul 2023 09:05
    Last modified:20 Apr 2024 00:54
    URI:https://strathprints.strath.ac.uk/id/eprint/86295
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