Second Messenger-Mediated Adjustment of Bacterial Swimming Velocity

Bacteria swim by means of rotating flagella that are powered by ion influx through membrane-spanning motor complexes. Escherichia coli and related species harness a chemosensory and signal transduction machinery that governs the direction of flagellar rotation and allows them to navigate in chemical...

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Bibliographic Details
Published in:Cell 2010-04, Vol.141 (1), p.107-116
Main Authors: Boehm, Alex, Kaiser, Matthias, Li, Hui, Spangler, Christian, Kasper, Christoph Alexander, Ackermann, Martin, Kaever, Volkhard, Sourjik, Victor, Roth, Volker, Jenal, Urs
Format: Article
Language:English
Subjects:
Adaptations
Amino Acid Sequence
Bacterial Proteins - metabolism
CELLBIO
Cyclic GMP - analogs & derivatives
Cyclic GMP - metabolism
Escherichia coli
Escherichia coli - physiology
Escherichia coli Proteins - metabolism
Flagella - metabolism
MICROBIO
Molecular Sequence Data
Movement
Phosphorus-Oxygen Lyases - metabolism
Second Messenger Systems
Sequence Alignment
SIGNALING
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Summary:Bacteria swim by means of rotating flagella that are powered by ion influx through membrane-spanning motor complexes. Escherichia coli and related species harness a chemosensory and signal transduction machinery that governs the direction of flagellar rotation and allows them to navigate in chemical gradients. Here, we show that Escherichia coli can also fine-tune its swimming speed with the help of a molecular brake (YcgR) that, upon binding of the nucleotide second messenger cyclic di-GMP, interacts with the motor protein MotA to curb flagellar motor output. Swimming velocity is controlled by the synergistic action of at least five signaling proteins that adjust the cellular concentration of cyclic di-GMP. Activation of this network and the resulting deceleration coincide with nutrient depletion and might represent an adaptation to starvation. These experiments demonstrate that bacteria can modulate flagellar motor output and thus swimming velocity in response to environmental cues. [Display omitted] ► Concentration of second messenger cyclic di-GMP sets bacterial swimming velocity ► Upon cyclic di-GMP binding, YcgR interacts with the flagellar motor protein MotA ► YcgR binding to MotA acts to curb motor output in a brake-like fashion ► Pathway activation and resulting deceleration coincide with nutrient depletion
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2010.01.018