Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries

Akihiro Kawamoto, Tomoko Miyata, Fumiaki Makino, Miki Kinoshita, Tohru Minamino, Katsumi Imada, Takayuki Kato () and Keiichi Namba ()
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Akihiro Kawamoto: Osaka University
Tomoko Miyata: Osaka University
Fumiaki Makino: Osaka University
Miki Kinoshita: Osaka University
Tohru Minamino: Osaka University
Katsumi Imada: Osaka University
Takayuki Kato: Osaka University
Keiichi Namba: Osaka University

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque generation and rotation switch, and a large symmetry mismatch between these two rings has been a long puzzle, especially with respect to their role in motor function. Here, using cryoEM structural analysis of the flagellar basal body and the MS ring formed by full-length FliF from Salmonella enterica, we show that the native MS ring is formed by 34 FliF subunits with no symmetry variation. Symmetry analysis of the C ring shows a variation with a peak at 34-fold, suggesting flexibility in C ring assembly. Finally, our data also indicate that FliF subunits assume two different conformations, contributing differentially to the inner and middle parts of the M ring and thus resulting in 23- and 11-fold subsymmetries in the inner and middle M ring, respectively. The internal core of the M ring, formed by 23 subunits, forms a hole of the right size to accommodate the protein export gate.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24507-9

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DOI: 10.1038/s41467-021-24507-9

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