ArticleJournal of bacteriology2005
Deletion analysis of the carboxyl-terminal region of the PomB component of the vibrio alginolyticus polar flagellar motor.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Characterization of the periplasmic region of PomB, a Na+-driven flagellar stator protein in Vibrio alginolyticus.Journal of bacteriology · 2011Article
- Structure of the flagellar motor protein complex PomAB: implications for the torque-generating conformation.Journal of bacteriology · 2011Article
- Characterization of the periplasmic domain of MotB and implications for its role in the stator assembly of the bacterial flagellar motor.Journal of bacteriology · 2008Article
- Crystallization and preliminary X-ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
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Authors and funding
3 authors.
Funding
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Abstract
The stator of the sodium-driven flagellar motor of Vibrio alginolyticus is a membrane protein complex composed of four PomA and two PomB subunits. PomB has a peptidoglycan-binding motif in the C-terminal region. In this study, four kinds of PomB deletions in the C terminus were constructed. None of the deletion proteins restored motility of the DeltapomB strain. The PomA protein was coisolated with all of the PomB derivatives under detergent-solubilized conditions. Homotypic disulfide cross-linking of all of the deletion derivatives through naturally occurring Cys residues was detected. We conclude that the C-terminal region of PomB is essential for motor function but not for oligomerization of PomB with itself or PomA.
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