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  The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH

Halang, P., Leptihn, S., Meier, T., Vorburger, T., & Steuber, J. (2013). The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH. Journal of Bacteriology, 195(21), 4888-4899. doi:10.1128/JB.00353-13.

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 Creators:
Halang, Petra1, Author
Leptihn, Sebastian1, Author
Meier, Thomas2, 3, Author           
Vorburger, Thomas1, Author
Steuber, Julia1, Author
Affiliations:
1Institute of Microbiology, University of Hohenheim (Stuttgart), Stuttgart, Germany, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Cluster of Excellence Macromolecular Complexes, Goethe University, Frankfurt am Main, Germany, ou_persistent22              

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 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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Language(s): eng - English
 Dates: 2013-03-282013-08-202013-08-232013-11-01
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1128/JB.00353-13
PMID: 23974033
PMC: 3807483
 Degree: -

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Title: Journal of Bacteriology
  Other : J. Bacteriol.
Source Genre: Journal
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Publ. Info: Washington, DC : American Society for Microbiology (ASM)
Pages: - Volume / Issue: 195 (21) Sequence Number: - Start / End Page: 4888 - 4899 Identifier: ISSN: 0021-9193
CoNE: https://pure.mpg.de/cone/journals/resource/954925410823