Publication Date:
2010-02-06
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bai, Fan -- Branch, Richard W -- Nicolau, Dan V Jr -- Pilizota, Teuta -- Steel, Bradley C -- Maini, Philip K -- Berry, Richard M -- BB/E00458X/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/H01991X/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2010 Feb 5;327(5966):685-9. doi: 10.1126/science.1182105.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20133571" target="_blank"〉PubMed〈/a〉
Keywords:
Allosteric Regulation
;
Bacterial Proteins/chemistry/metabolism
;
Binding Sites
;
Escherichia coli/metabolism
;
Escherichia coli Proteins/*chemistry/*metabolism
;
Flagella/*chemistry
;
Membrane Proteins/chemistry/metabolism
;
Models, Biological
;
Models, Molecular
;
Molecular Motor Proteins/*chemistry/*metabolism
;
Monte Carlo Method
;
Protein Binding
;
Protein Conformation
;
Protein Subunits/*chemistry/*metabolism
;
Signal Transduction
;
Thermodynamics
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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