Evidence for Two Flagellar Stators and Their Role in the Motility of
            <i>Pseudomonas aeruginosa</i>

Toutain, Christine M.; Zegans, Michael E.; O’Toole, George A.

doi:10.1128/jb.187.2.771-777.2005

Cited by 160 publications

(217 citation statements)

References 52 publications

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“…5b). The motA and motB genes encode proteins that make up the stator or stationary component of the flagellar motor (Toutain et al, 2005). Expression of motA and motB was down twofold in the rsmA mutant compared to PAO1 (Table 2).…”

Section: Resultsmentioning

confidence: 99%

Influence of the regulatory protein RsmA on cellular functions in Pseudomonas aeruginosa PAO1, as revealed by transcriptome analysis

et al. 2006

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RsmA is a posttranscriptional regulatory protein in Pseudomonas aeruginosa that works in tandem with a small non-coding regulatory RNA molecule, RsmB (RsmZ), to regulate the expression of several virulence-related genes, including the N-acyl-homoserine lactone synthase genes lasI and rhlI, and the hydrogen cyanide and rhamnolipid biosynthetic operons. Although these targets of direct RsmA regulation have been identified, the full impact of RsmA on cellular activities is not as yet understood. To address this issue the transcriptome profiles of P. aeruginosa PAO1 and an isogenic rsmA mutant were compared. Loss of RsmA altered the expression of genes involved in a variety of pathways and systems important for virulence, including iron acquisition, biosynthesis of the Pseudomonas quinolone signal (PQS), the formation of multidrug efflux pumps, and motility. Not all of these effects can be explained through the established regulatory roles of RsmA. This study thus provides both a first step towards the identification of further genes under RsmA posttranscriptional control in P. aeruginosa and a fuller understanding of the broader impact of RsmA on cellular functions.

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Section: Resultsmentioning

confidence: 99%

Influence of the regulatory protein RsmA on cellular functions in Pseudomonas aeruginosa PAO1, as revealed by transcriptome analysis

et al. 2006

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“…Evidence for this was provided by several research laboratories (92,155,156,163) and is exemplified by findings of Van Dellen et al (160) demonstrating that while V. cholerae O139 flagellar mutants show reduced attachment, they eventually form a robust monolayer biofilm. In contrast, monolayer formation was severely impaired in the absence of the flagellar motor.…”

Section: The First Contactmentioning

confidence: 92%

“…The P. aeruginosa genome encodes only one flagellum and one motor but two flagellar stators, MotAB and MotCD, which are the static elements of the bacterial motor, providing energy to turn this appendage and therefore propel the cell through its environment. While either flagellar stator is sufficient for swimming, both are necessary for surface-associated swarming motility (156). Moreover, mutations in either MotAB or MotCD render P. aeruginosa defective in attachment in both static and flow cell systems.…”

Section: The First Contactmentioning

confidence: 99%

Sticky Situations: Key Components That Control Bacterial Surface Attachment

Petrova

Sauer

2012

Journal of Bacteriology

313

251

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“…Thus, P. aeruginosa PAO1 harbours MotAB and MotCD, which power a single polar flagellum by an unknown mechanism (Doyle et al, 2004;Toutain et al, 2005), while B. subtilis and S. oneidensis MR-1 harbour stator complexes with different ion specificities (Ito et al, 2004;Paulick et al, 2009). B. subtilis MotAB and S. oneidensis MotAB-MotXY are proton-driven, whereas B. subtilis MotPS and S. oneidensis PomAB-MotXY are sodium-driven.…”

Section: Introductionmentioning

confidence: 99%

Aeromonas hydrophila motY is essential for polar flagellum function, and requires coordinate expression of motX and Pom proteins

et al. 2011

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By the analysis of the Aeromonas hydrophila ATCC7966T genome we identified A. hydrophila AH-3 MotY. A. hydrophila MotY, like MotX, is essential for the polar flagellum function energized by an electrochemical potential of Na+ as coupling ion, but is not involved in lateral flagella function energized by the proton motive force. Thus, the A. hydrophila polar flagellum stator is a complex integrated by two essential proteins, MotX and MotY, which interact with one of two redundant pairs of proteins, PomAB and PomA2B2. In an A. hydrophila motX mutant, polar flagellum motility is restored by motX complementation, but the ability of the A. hydrophila motY mutant to swim is not restored by introduction of the wild-type motY alone. However, its polar flagellum motility is restored when motX and -Y are expressed together from the same plasmid promoter. Finally, even though both the redundant A. hydrophila polar flagellum stators, PomAB and PomA2B2, are energized by the Na+ ion, they cannot be exchanged. Furthermore, Vibrio parahaemolyticus PomAB and Pseudomonas aeruginosa MotAB or MotCD are unable to restore swimming motility in A. hydrophila polar flagellum stator mutants.

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Evidence for Two Flagellar Stators and Their Role in the Motility of Pseudomonas aeruginosa

Cited by 160 publications

References 52 publications

Influence of the regulatory protein RsmA on cellular functions in Pseudomonas aeruginosa PAO1, as revealed by transcriptome analysis

Influence of the regulatory protein RsmA on cellular functions in Pseudomonas aeruginosa PAO1, as revealed by transcriptome analysis

Sticky Situations: Key Components That Control Bacterial Surface Attachment

Aeromonas hydrophila motY is essential for polar flagellum function, and requires coordinate expression of motX and Pom proteins

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