ArticleBMC microbiology2024
MotY modulates proton-driven flagellar motor output in Pseudomonas aeruginosa.
Article in BMC microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
6 authors.
Funding
Abstract
MotY homologs are present in a variety of monotrichous bacterial strains and are thought to form an additional structural T ring in flagellar motors. While MotY potentially plays an important role in motor torque generation, its impact on motor output dynamics remains poorly understood. In this study, we investigate the role of MotY in P. aeruginosa, elucidating its interactions with the two sets of stator units (MotAB and MotCD) using Förster resonance energy transfer (FRET) assays. Employing a newly developed bead assay, we characterize the dynamic behavior of flagellar motors in motY mutants, identifying MotY as the key functional protein to affect the clockwise bias of naturally unbiased motors in P. aeruginosa. Our findings reveal that MotY enhances stator assembly efficiency without affecting the overall assembly of the flagellar structure. Additionally, we demonstrate that MotY is essential for maintaining motor torque and regulating switching rates. Our study highlights the physiological significance of MotY in fine-tuning flagellar motor function in complex environments.
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