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Conformational Spread as a Mechanism for Cooperativity in the Bacterial Flagellar Switch
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Conformational Spread as a Mechanism for Cooperativity in the Bacterial Flagellar Switch
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Journal Article
Conformational Spread as a Mechanism for Cooperativity in the Bacterial Flagellar Switch
2010
Overview
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.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biological and medical sciences
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Ligands
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Methyl-Accepting Chemotaxis Proteins
/ Modeling
/ Molecular Motor Proteins - chemistry
/ Molecular Motor Proteins - metabolism
/ Protein Subunits - chemistry
/ Protein Subunits - metabolism
/ Rotation
