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Functional role of a conserved aspartic acid residue in the motor of the Na(+)-driven flagellum from Vibrio cholerae


Vorburger, T; Stein, A; Ziegler, U; Kaim, G; Steuber, J (2009). Functional role of a conserved aspartic acid residue in the motor of the Na(+)-driven flagellum from Vibrio cholerae. Biochimica et Biophysica Acta, 1787(10):1198-1204.

Abstract

The flagellar motor consists of a rotor and a stator and couples the flux of cations (H(+) or Na(+)) to the generation of the torque necessary to drive flagellum rotation. The inner membrane proteins PomA and PomB are stator components of the Na(+)-driven flagellar motor from Vibrio cholerae. Affinity-tagged variants of PomA and PomB were co-expressed in trans in the non-motile V. cholerae pomAB deletion strain to study the role of the conserved D23 in the transmembrane helix of PomB. At pH 9, the D23E variant restored motility to 100% of that observed with wild type PomB, whereas the D23N variant resulted in a non-motile phenotype, indicating that a carboxylic group at position 23 in PomB is important for flagellum rotation. Motility tests at decreasing pH revealed a pronounced decline of flagellar function with a motor complex containing the PomB-D23E variant. It is suggested that the protonation state of the glutamate residue at position 23 determines the performance of the flagellar motor by altering the affinity of Na(+) to PomB. The conserved aspartate residue in the transmembrane helix of PomB and its H(+)-dependent homologs might act as a ligand for the coupling cation in the flagellar motor.

Abstract

The flagellar motor consists of a rotor and a stator and couples the flux of cations (H(+) or Na(+)) to the generation of the torque necessary to drive flagellum rotation. The inner membrane proteins PomA and PomB are stator components of the Na(+)-driven flagellar motor from Vibrio cholerae. Affinity-tagged variants of PomA and PomB were co-expressed in trans in the non-motile V. cholerae pomAB deletion strain to study the role of the conserved D23 in the transmembrane helix of PomB. At pH 9, the D23E variant restored motility to 100% of that observed with wild type PomB, whereas the D23N variant resulted in a non-motile phenotype, indicating that a carboxylic group at position 23 in PomB is important for flagellum rotation. Motility tests at decreasing pH revealed a pronounced decline of flagellar function with a motor complex containing the PomB-D23E variant. It is suggested that the protonation state of the glutamate residue at position 23 determines the performance of the flagellar motor by altering the affinity of Na(+) to PomB. The conserved aspartate residue in the transmembrane helix of PomB and its H(+)-dependent homologs might act as a ligand for the coupling cation in the flagellar motor.

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3 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2009
Deposited On:27 Jul 2009 12:33
Last Modified:05 Apr 2016 13:18
Publisher:Elsevier
ISSN:0006-3002
Publisher DOI:https://doi.org/10.1016/j.bbabio.2009.05.015
PubMed ID:19501041

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