Conformational Spread as a Mechanism for Cooperativity in the Bacterial Flagellar Switch

被引：153

作者：

Bai, Fan ^{[1
,2
]}

Branch, Richard W. ^{[1
]}

Nicolau, Dan V., Jr. ^{[3
,4
]}

Pilizota, Teuta ^{[1
,5
]}

Steel, Bradley C. ^{[1
]}

Maini, Philip K. ^{[3
,6
]}

Berry, Richard M. ^{[1
]}

机构：

[1] Univ Oxford, Dept Phys, Clarendon Lab, Oxford OX1 3PU, England

[2] Osaka Univ, Grad Sch Frontier Biosci, Nanobiol Labs, Suita, Osaka 5650871, Japan

[3] Univ Oxford, Inst Math, Ctr Math Biol, Oxford OX1 3LB, England

[4] Univ Calif Berkeley, Dept Integrat Biol, Berkeley, CA 94708 USA

[5] Princeton Univ, Carl Icahn Lab, Princeton, NJ 08644 USA

[6] Univ Oxford, Dept Biochem, Oxford Ctr Integrat Syst Biol, Oxford OX1 3QU, England

来源：

SCIENCE | 2010年 / 327卷 / 5966期

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;

关键词：

TORQUE-GENERATING UNITS; RESPONSE REGULATOR CHEY; ESCHERICHIA-COLI; ALLOSTERIC MECHANISMS; MOTOR; CHEMOTAXIS; PROTEINS; ROTATION; BINDING; COMPLEX;

D O I：

10.1126/science.1182105

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The bacterial flagellar switch that controls the direction of flagellar rotation during chemotaxis has a highly cooperative response. This has previously been understood in terms of the classic two-state, concerted model of allosteric regulation. Here, we used high-resolution optical microscopy to observe switching of single motors and uncover the stochastic multistate nature of the switch. Our observations are in detailed quantitative agreement with a recent general model of allosteric cooperativity that exhibits conformational spread-the stochastic growth and shrinkage of domains of adjacent subunits sharing a particular conformational state. We expect that conformational spread will be important in explaining cooperativity in other large signaling complexes.

引用

页码：685 / 689

页数：5

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