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The FlhA linker mediates flagellar protein export switching during flagellar assembly

The flagellar protein export apparatus switches substrate specificity from hook-type to filament-type upon hook assembly completion, thereby initiating filament assembly at the hook tip. The C-terminal cytoplasmic domain of FlhA (FlhA(C)) serves as a docking platform for flagellar chaperones in comp...

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Autores principales: Inoue, Yumi, Kinoshita, Miki, Kida, Mamoru, Takekawa, Norihiro, Namba, Keiichi, Imada, Katsumi, Minamino, Tohru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8166844/
https://www.ncbi.nlm.nih.gov/pubmed/34059784
http://dx.doi.org/10.1038/s42003-021-02177-z
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author Inoue, Yumi
Kinoshita, Miki
Kida, Mamoru
Takekawa, Norihiro
Namba, Keiichi
Imada, Katsumi
Minamino, Tohru
author_facet Inoue, Yumi
Kinoshita, Miki
Kida, Mamoru
Takekawa, Norihiro
Namba, Keiichi
Imada, Katsumi
Minamino, Tohru
author_sort Inoue, Yumi
collection PubMed
description The flagellar protein export apparatus switches substrate specificity from hook-type to filament-type upon hook assembly completion, thereby initiating filament assembly at the hook tip. The C-terminal cytoplasmic domain of FlhA (FlhA(C)) serves as a docking platform for flagellar chaperones in complex with their cognate filament-type substrates. Interactions of the flexible linker of FlhA (FlhA(L)) with its nearest FlhA(C) subunit in the FlhA(C) ring is required for the substrate specificity switching. To address how FlhA(L) brings the order to flagellar assembly, we analyzed the flhA(E351A/W354A/D356A) ΔflgM mutant and found that this triple mutation in FlhA(L) increased the secretion level of hook protein by 5-fold, thereby increasing hook length. The crystal structure of FlhA(C)(E351A/D356A) showed that FlhA(L) bound to the chaperone-binding site of its neighboring subunit. We propose that the interaction of FlhA(L) with the chaperon-binding site of FlhA(C) suppresses filament-type protein export and facilitates hook-type protein export during hook assembly.
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spelling pubmed-81668442021-06-15 The FlhA linker mediates flagellar protein export switching during flagellar assembly Inoue, Yumi Kinoshita, Miki Kida, Mamoru Takekawa, Norihiro Namba, Keiichi Imada, Katsumi Minamino, Tohru Commun Biol Article The flagellar protein export apparatus switches substrate specificity from hook-type to filament-type upon hook assembly completion, thereby initiating filament assembly at the hook tip. The C-terminal cytoplasmic domain of FlhA (FlhA(C)) serves as a docking platform for flagellar chaperones in complex with their cognate filament-type substrates. Interactions of the flexible linker of FlhA (FlhA(L)) with its nearest FlhA(C) subunit in the FlhA(C) ring is required for the substrate specificity switching. To address how FlhA(L) brings the order to flagellar assembly, we analyzed the flhA(E351A/W354A/D356A) ΔflgM mutant and found that this triple mutation in FlhA(L) increased the secretion level of hook protein by 5-fold, thereby increasing hook length. The crystal structure of FlhA(C)(E351A/D356A) showed that FlhA(L) bound to the chaperone-binding site of its neighboring subunit. We propose that the interaction of FlhA(L) with the chaperon-binding site of FlhA(C) suppresses filament-type protein export and facilitates hook-type protein export during hook assembly. Nature Publishing Group UK 2021-05-31 /pmc/articles/PMC8166844/ /pubmed/34059784 http://dx.doi.org/10.1038/s42003-021-02177-z Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Inoue, Yumi
Kinoshita, Miki
Kida, Mamoru
Takekawa, Norihiro
Namba, Keiichi
Imada, Katsumi
Minamino, Tohru
The FlhA linker mediates flagellar protein export switching during flagellar assembly
title The FlhA linker mediates flagellar protein export switching during flagellar assembly
title_full The FlhA linker mediates flagellar protein export switching during flagellar assembly
title_fullStr The FlhA linker mediates flagellar protein export switching during flagellar assembly
title_full_unstemmed The FlhA linker mediates flagellar protein export switching during flagellar assembly
title_short The FlhA linker mediates flagellar protein export switching during flagellar assembly
title_sort flha linker mediates flagellar protein export switching during flagellar assembly
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8166844/
https://www.ncbi.nlm.nih.gov/pubmed/34059784
http://dx.doi.org/10.1038/s42003-021-02177-z
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