ArticleJournal of bacteriology2013
The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH.
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 8 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
8 citing papers in PubMed, 11 citations in OpenAlex.
- Advances in cholera research: from molecular biology to public health initiatives.Frontiers in microbiology · 2023Review
- Voltage vs. Ligand II: Structural insights of the intrinsic flexibility in cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2019Article
- Article
- The Na+-Translocating NADH:Quinone Oxidoreductase Enhances Oxidative Stress in the Cytoplasm of Vibrio cholerae.Journal of bacteriology · 2016Article
- The Ecological Coherence of Temperature and Salinity Tolerance Interaction and Pigmentation in a Non-marineFrontiers in microbiology · 2016Article
- Response of Vibrio cholerae to the Catecholamine Hormones Epinephrine and Norepinephrine.Journal of bacteriology · 2015Article
- Serine 26 in the PomB subunit of the flagellar motor is essential for hypermotility of Vibrio cholerae.PloS one · 2015Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio cholerae is motile by its polar flagellum, which is driven by a Na(+)-conducting motor. The stators of the motor, composed of four PomA and two PomB subunits, provide access for Na(+) to the torque-generating unit of the motor. To characterize the Na(+) pathway formed by the PomAB complex, we studied the influence of chloride salts (chaotropic, Na(+), and K(+)) and pH on the motility of V. cholerae. Motility decreased at elevated pH but increased if a chaotropic chloride salt was added, which rules out a direct Na(+) and H(+) competition in the process of binding to the conserved PomB D23 residue. Cells expressing the PomB S26A/T or D42N variants lost motility at low Na(+) concentrations but regained motility in the presence of 170 mM chloride. Both PomA and PomB were modified by N,N'-dicyclohexylcarbodiimide (DCCD), indicating the presence of protonated carboxyl groups in the hydrophobic regions of the two proteins. Na(+) did not protect PomA and PomB from this modification. Our study shows that both osmolality and pH have an influence on the function of the flagellum from V. cholerae. We propose that D23, S26, and D42 of PomB are part of an ion-conducting pathway formed by the PomAB stator complex.
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Registered trials
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.