ArticleJournal of bacteriology2000
A slow-motility phenotype caused by substitutions at residue Asp31 in the PomA channel component of a sodium-driven flagellar motor.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed, 22 citations in OpenAlex.
- Ion-Powered Rotary Motors: Where Did They Come from and Where They Are Going?International journal of molecular sciences · 2023Review
- The rapid evolution of flagellar ion selectivity in experimental populations ofScience advances · 2022Article
- Putative Spanner Function of theJournal of bacteriology · 2021Article
- Essential ion binding residues for NaScientific reports · 2019Article
- Comparative study of the ion flux pathway in stator units of proton- and sodium-driven flagellar motors.Biophysics (Nagoya-shi, Japan) · 2009Article
- Interaction of PomB with the third transmembrane segment of PomA in the Na+-driven polar flagellum of Vibrio alginolyticus.Journal of bacteriology · 2004Article
- Polar flagellar motility of the Vibrionaceae.Microbiology and molecular biology reviews : MMBR · 2001Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PomA is thought to be a component of the ion channel in the sodium-driven polar-flagellar motor of Vibrio alginolyticus. We have found that some cysteine substitutions in the periplasmic region of PomA result in a slow-motility phenotype, in which swarming and swimming speeds are reduced even in the presence of high concentrations of NaCl. Most of the mutants showed a sodium ion dependence similar to that of the wild type but with significantly reduced motility at all sodium ion concentrations. By contrast, motility of the D31C mutant showed a sharp dependence on NaCl concentration, with a threshold at 38 mM. The motor of the D31C mutant rotates stably, as monitored by laser dark-field microscopy, suggesting that the mutant PomA protein is assembled normally into the motor complex. Mutational studies of Asp31 suggest that, although this residue is not essential for motor rotation, a negative charge at this position contributes to optimal speed and/or efficiency of the motor.
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