Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.

Flagella, the primary means of motility in bacteria, are helical filaments that function as microscopic propellers composed of thousands of copies of the protein flagellin. Here, we show that many bacteria encode "giant" flagellins, greater than a thousand amino acids in length, and that t...

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Main Authors: Nicholas M Thomson, Josie L Ferreira, Teige R Matthews-Palmer, Morgan Beeby, Mark J Pallen
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2018-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC6248924?pdf=render
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author Nicholas M Thomson
Josie L Ferreira
Teige R Matthews-Palmer
Morgan Beeby
Mark J Pallen
author_facet Nicholas M Thomson
Josie L Ferreira
Teige R Matthews-Palmer
Morgan Beeby
Mark J Pallen
author_sort Nicholas M Thomson
collection DOAJ
description Flagella, the primary means of motility in bacteria, are helical filaments that function as microscopic propellers composed of thousands of copies of the protein flagellin. Here, we show that many bacteria encode "giant" flagellins, greater than a thousand amino acids in length, and that two species that encode giant flagellins, the marine γ-proteobacteria Bermanella marisrubri and Oleibacter marinus, produce monopolar flagellar filaments considerably thicker than filaments composed of shorter flagellin monomers. We confirm that the flagellum from B. marisrubri is built from its giant flagellin. Phylogenetic analysis reveals that the mechanism of evolution of giant flagellins has followed a stepwise process involving an internal domain duplication followed by insertion of an additional novel insert. This work illustrates how "the" bacterial flagellum should not be seen as a single, idealised structure, but as a continuum of evolved machines adapted to a range of niches.
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spelling doaj.art-2a1b6c823e424b43a9a462bbfdc3df0e2022-12-21T20:36:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032018-01-011311e020654410.1371/journal.pone.0206544Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.Nicholas M ThomsonJosie L FerreiraTeige R Matthews-PalmerMorgan BeebyMark J PallenFlagella, the primary means of motility in bacteria, are helical filaments that function as microscopic propellers composed of thousands of copies of the protein flagellin. Here, we show that many bacteria encode "giant" flagellins, greater than a thousand amino acids in length, and that two species that encode giant flagellins, the marine γ-proteobacteria Bermanella marisrubri and Oleibacter marinus, produce monopolar flagellar filaments considerably thicker than filaments composed of shorter flagellin monomers. We confirm that the flagellum from B. marisrubri is built from its giant flagellin. Phylogenetic analysis reveals that the mechanism of evolution of giant flagellins has followed a stepwise process involving an internal domain duplication followed by insertion of an additional novel insert. This work illustrates how "the" bacterial flagellum should not be seen as a single, idealised structure, but as a continuum of evolved machines adapted to a range of niches.http://europepmc.org/articles/PMC6248924?pdf=render
spellingShingle Nicholas M Thomson
Josie L Ferreira
Teige R Matthews-Palmer
Morgan Beeby
Mark J Pallen
Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.
PLoS ONE
title Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.
title_full Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.
title_fullStr Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.
title_full_unstemmed Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.
title_short Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria.
title_sort giant flagellins form thick flagellar filaments in two species of marine γ proteobacteria
url http://europepmc.org/articles/PMC6248924?pdf=render
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