FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis
Abstract
Flagellin is amongst the most abundant proteins in flagellated bacterial species and constitutes the major building block of the flagellar filament. The proteins FliW and FliS serve in the post-transcriptional control of flagellin and guide the protein to the flagellar type III secretion system (fT3SS), respectively. Here, we present the high-resolution structure of FliS/flagellin heterodimer and show that FliS and FliW bind to opposing interfaces located at the N- and C-termini of flagellin. The FliS/flagellin/FliW heterotrimer is able to interact with FlhA-C suggesting that FliW and FliS are released during flagellin export. After release, FliW and FliS are recycled to execute a new round of post-transcriptional regulation and targeting. Taken together, our study provides a mechanism explaining how FliW and FliS synchronize the production of flagellin with the capacity of the fT3SS to secrete flagellin.
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BibTeX
@article{altegoer2026flisflagellinfliw,
title = {{FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis}},
author = {Florian Altegoer and Sampriti Mukherjee and Wieland Steinchen and Patricia Bedrunka and Uwe Linne and Daniel B. Kearns and Gert Bange},
journal = {Scientific Reports},
year = {2026},
month = oct,
doi = {10.1038/s41598-018-29884-8},
url = {https://hal.science/hal-05780536v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis
AU - Florian Altegoer
AU - Sampriti Mukherjee
AU - Wieland Steinchen
AU - Patricia Bedrunka
AU - Uwe Linne
AU - Daniel B. Kearns
AU - Gert Bange
PY - 2026
DA - 2026/10/06
JO - Scientific Reports
DO - 10.1038/s41598-018-29884-8
UR - https://hal.science/hal-05780536v1
AB - Flagellin is amongst the most abundant proteins in flagellated bacterial species and constitutes the major building block of the flagellar filament. The proteins FliW and FliS serve in the post-transcriptional control of flagellin and guide the protein to the flagellar type III secretion system (fT3SS), respectively. Here, we present the high-resolution structure of FliS/flagellin heterodimer and show that FliS and FliW bind to opposing interfaces located at the N- and C-termini of flagellin. The FliS/flagellin/FliW heterotrimer is able to interact with FlhA-C suggesting that FliW and FliS are released during flagellin export. After release, FliW and FliS are recycled to execute a new round of post-transcriptional regulation and targeting. Taken together, our study provides a mechanism explaining how FliW and FliS synchronize the production of flagellin with the capacity of the fT3SS to secrete flagellin.
SN - 2045-2322
ER -