Conformational spread as a mechanism for cooperativity in the bacterial flagellar switch
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.
| Errataetall: |
CommentIn: Science. 2010 Feb 5;327(5966):653-4. - PMID 20133562 |
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| Medienart: |
E-Artikel |
| Erscheinungsjahr: |
2010 |
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| Erschienen: |
2010 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:327 |
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| Enthalten in: |
Science (New York, N.Y.) - 327(2010), 5966 vom: 05. Feb., Seite 685-9 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Bai, Fan [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 24.02.2010 Date Revised 20.10.2021 published: Print CommentIn: Science. 2010 Feb 5;327(5966):653-4. - PMID 20133562 Citation Status MEDLINE |
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| doi: |
10.1126/science.1182105 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM194889491 |
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| 500 | |a published: Print | ||
| 500 | |a CommentIn: Science. 2010 Feb 5;327(5966):653-4. - PMID 20133562 | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Bacterial Proteins |2 NLM | |
| 650 | 7 | |a Escherichia coli Proteins |2 NLM | |
| 650 | 7 | |a FliN protein, Bacteria |2 NLM | |
| 650 | 7 | |a Flig protein, Bacteria |2 NLM | |
| 650 | 7 | |a Membrane Proteins |2 NLM | |
| 650 | 7 | |a Methyl-Accepting Chemotaxis Proteins |2 NLM | |
| 650 | 7 | |a Molecular Motor Proteins |2 NLM | |
| 650 | 7 | |a Protein Subunits |2 NLM | |
| 650 | 7 | |a FliM protein, Bacteria |2 NLM | |
| 650 | 7 | |a 134548-59-7 |2 NLM | |
| 700 | 1 | |a Branch, Richard W |e verfasserin |4 aut | |
| 700 | 1 | |a Nicolau, Dan V |c Jr |e verfasserin |4 aut | |
| 700 | 1 | |a Pilizota, Teuta |e verfasserin |4 aut | |
| 700 | 1 | |a Steel, Bradley C |e verfasserin |4 aut | |
| 700 | 1 | |a Maini, Philip K |e verfasserin |4 aut | |
| 700 | 1 | |a Berry, Richard M |e verfasserin |4 aut | |
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