rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5966
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pubmed:dateCreated |
2010-2-5
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FliM protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/FliN protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Flig protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/methyl-accepting chemotaxis proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-9203
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
5
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pubmed:volume |
327
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
685-9
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pubmed:meshHeading |
pubmed-meshheading:20133571-Allosteric Regulation,
pubmed-meshheading:20133571-Bacterial Proteins,
pubmed-meshheading:20133571-Binding Sites,
pubmed-meshheading:20133571-Escherichia coli,
pubmed-meshheading:20133571-Escherichia coli Proteins,
pubmed-meshheading:20133571-Flagella,
pubmed-meshheading:20133571-Membrane Proteins,
pubmed-meshheading:20133571-Models, Biological,
pubmed-meshheading:20133571-Models, Molecular,
pubmed-meshheading:20133571-Molecular Motor Proteins,
pubmed-meshheading:20133571-Monte Carlo Method,
pubmed-meshheading:20133571-Protein Binding,
pubmed-meshheading:20133571-Protein Conformation,
pubmed-meshheading:20133571-Protein Subunits,
pubmed-meshheading:20133571-Signal Transduction,
pubmed-meshheading:20133571-Thermodynamics
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pubmed:year |
2010
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pubmed:articleTitle |
Conformational spread as a mechanism for cooperativity in the bacterial flagellar switch.
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pubmed:affiliation |
Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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