Mechanism for adaptive remodeling of the bacterial flagellar switch
The bacterial flagellar motor has been shown in previous work to adapt to changes in the steady-state concentration of the chemotaxis signaling molecule, CheY-P, by changing the FliM content. We show here that the number of FliM molecules in the motor and the fraction of FliM molecules that exchange depend on the direction of flagellar rotation, not on CheY-P binding per se. Our results are consistent with a model in which the structural differences associated with the direction of rotation modulate the strength of FliM binding. When the motor spins counterclockwise, FliM binding strengthens, the fraction of FliM molecules that exchanges decreases, and the ring content increases. The larger number of CheY-P binding sites enhances the motor's sensitivity, i.e., the motor adapts. An interesting unresolved question is how additional copies of FliM might be accommodated.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2012 |
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| Erschienen: |
2012 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:109 |
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| Enthalten in: |
Proceedings of the National Academy of Sciences of the United States of America - 109(2012), 49 vom: 04. Dez., Seite 20018-22 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Lele, Pushkar P [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 06.02.2013 Date Revised 03.12.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1073/pnas.1212327109 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM222790334 |
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| 100 | 1 | |a Lele, Pushkar P |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Mechanism for adaptive remodeling of the bacterial flagellar switch |
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| 500 | |a Date Revised 03.12.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a The bacterial flagellar motor has been shown in previous work to adapt to changes in the steady-state concentration of the chemotaxis signaling molecule, CheY-P, by changing the FliM content. We show here that the number of FliM molecules in the motor and the fraction of FliM molecules that exchange depend on the direction of flagellar rotation, not on CheY-P binding per se. Our results are consistent with a model in which the structural differences associated with the direction of rotation modulate the strength of FliM binding. When the motor spins counterclockwise, FliM binding strengthens, the fraction of FliM molecules that exchanges decreases, and the ring content increases. The larger number of CheY-P binding sites enhances the motor's sensitivity, i.e., the motor adapts. An interesting unresolved question is how additional copies of FliM might be accommodated | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
| 650 | 7 | |a Bacterial Proteins |2 NLM | |
| 650 | 7 | |a Escherichia coli Proteins |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 cheY protein, E coli |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 Nathan, Vedhavalli S J |e verfasserin |4 aut | |
| 700 | 1 | |a Berg, Howard C |e verfasserin |4 aut | |
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