Second Messenger-Mediated Adjustment of Bacterial Swimming Velocity

被引：366

作者：

Boehm, Alex ^{[1
]}

Kaiser, Matthias ^{[1
]}

Li, Hui ^{[2
]}

Spangler, Christian ^{[3
]}

Kasper, Christoph Alexander ^{[1
]}

Ackermann, Martin ^{[4
,5
]}

Kaever, Volkhard ^{[3
]}

Sourjik, Victor ^{[2
]}

Roth, Volker ^{[6
]}

Jenal, Urs ^{[1
]}

机构：

[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland

[2] Univ Heidelberg, Zentrum Mol Biol, DKFZ ZMBH Alliance, D-69120 Heidelberg, Germany

[3] Hannover Med Sch, Inst Pharmacol, D-30625 Hannover, Germany

[4] ETH, Dept Environm Sci, CH-8092 Zurich, Switzerland

[5] EAWAG, Dept Environm Microbiol, CH-8092 Zurich, Switzerland

[6] Univ Basel, Dept Comp Sci, CH-4056 Basel, Switzerland

来源：

CELL | 2010年 / 141卷 / 01期

基金：

瑞士国家科学基金会;

关键词：

C-DI-GMP; FLAGELLAR ROTARY MOTOR; ESCHERICHIA-COLI; PILZ DOMAIN; IN-VIVO; MOTILITY; CHEMOTAXIS; PROTEINS; TORQUE; PATHWAY;

D O I：

10.1016/j.cell.2010.01.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：107 / 116

页数：10

共 35 条

[1] PilZ domain is part of the bacterial c-di-GMP binding protein [J].