ArticleJournal of bacteriology2013
A distant homologue of the FlgT protein interacts with MotB and FliL and is essential for flagellar rotation in Rhodobacter sphaeroides.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Article
- FliL and its paralog MotF have distinct roles in the stator activity of the Sinorhizobium meliloti flagellar motor.Molecular microbiology · 2022Article
- Swimming Using a Unidirectionally Rotating, Single Stopping Flagellum in the Alpha ProteobacteriumFrontiers in microbiology · 2022Review
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Characterization of FliL Proteins in Bradyrhizobium diazoefficiens: Lateral FliL Supports Swimming Motility, and Subpolar FliL Modulates the Lateral Flagellar System.Journal of bacteriology · 2020Article
- Structure ofmBio · 2019Article
- Characterization of FlgP, an Essential Protein for Flagellar Assembly inJournal of bacteriology · 2019Article
- FliL association with flagellar stator in the sodium-driven Vibrio motor characterized by the fluorescent microscopy.Scientific reports · 2018Article
- Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.Scientific reports · 2017Article
- Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural Characterization of the Fla2 Flagellum of Rhodobacter sphaeroides.Journal of bacteriology · 2015Article
- Loss of FliL alters Proteus mirabilis surface sensing and temperature-dependent swarming.Journal of bacteriology · 2015Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work, we describe a periplasmic protein that is essential for flagellar rotation in Rhodobacter sphaeroides. This protein is encoded upstream of flgA, and its expression is dependent on the flagellar master regulator FleQ and on the class III flagellar activator FleT. Sequence comparisons suggest that this protein is a distant homologue of FlgT. We show evidence that in R. sphaeroides, FlgT interacts with the periplasmic regions of MotB and FliL and with the flagellar protein MotF, which was recently characterized as a membrane component of the flagellum in this bacterium. In addition, the localization of green fluorescent protein (GFP)-MotF is completely dependent on FlgT. The Mot(-) phenotype of flgT cells was weakly suppressed by point mutants of MotB that presumably keep the proton channel open and efficiently suppress the Mot(-) phenotype of motF and fliL cells, indicating that FlgT could play an additional role beyond the opening of the proton channel. The presence of FlgT in purified filament-hook-basal bodies of the wild-type strain was confirmed by Western blotting, and the observation of these structures under an electron microscope showed that the basal bodies from flgT cells had lost the ring that covers the LP ring in the wild-type structure. Moreover, MotF was detected by immunoblotting in the basal bodies obtained from the wild-type strain but not from flgT cells. From these results, we suggest that FlgT forms a ring around the LP ring, which anchors MotF and stabilizes the stator complex of the flagellar motor.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.