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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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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. |
format | Online Article Text |
id | pubmed-8166844 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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