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...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-12, Vol.109 (49), p.20018-20022 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Lele, Pushkar P Branch, Richard W Nathan, Vedhavalli S. J Berg, Howard C |
| description | 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. |
| doi_str_mv | 10.1073/pnas.1212327109 |
| format | Article |
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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.</description><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding sites</subject><subject>Biological Sciences</subject><subject>Bleaching</subject><subject>Chemotaxis</subject><subject>Escherichia coli</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli - physiology</subject><subject>Flagella - physiology</subject><subject>flagellum</subject><subject>Fluorescence</subject><subject>Fluorescence Recovery After Photobleaching</subject><subject>Membrane Proteins - metabolism</subject><subject>Methyl-Accepting Chemotaxis Proteins</subject><subject>Microscopy, Fluorescence</subject><subject>Models, Chemical</subject><subject>Molecular Motor Proteins - metabolism</subject><subject>Molecules</subject><subject>Motors</subject><subject>Physiological regulation</subject><subject>Population growth</subject><subject>Protein Binding</subject><subject>Renovations</subject><subject>Rotation</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEQxS0EoqFw5gSsxIXLtjP-WvuChKLyIRVxgJ4tr-NNHO2ug70p4r-vl4QUuHCwPdL7zdOMHyHPES4QGna5G22-QIqU0QZBPyCLcmMtuYaHZAFAm1pxys_Ik5y3AKCFgsfkjDKUWgq9IMvP3m3sGPJQdTFVdmV3U7j1VfJDXPk-jOsqdtW08VVr3eRTsH3V9Xbt-96mKv8Ik9s8JY8622f_7Piek5v3V9-WH-vrLx8-Ld9d105onGrhOoXMSc0k6xonS2VdY6VjQtByBG9bob0ToDllXEghtGIMuPVCupaxc_L24Lvbt4NfOT9OyfZml8Jg008TbTB_K2PYmHW8Naz4K8qLwZujQYrf9z5PZgjZzauMPu6zQQUMFDZa_B-lZUSqUWBBX_-DbuM-jeUnflGKKYW6UJcHyqWYc_LdaW4EM2dp5izNfZal4-Wf65743-EVoDoCc-e9nTZcGwqAqiAvDsg2TzGdGF4k4GLWXx30zkZj1ylkc_OVAsrSzUCgZHdK4rX9</recordid><startdate>20121204</startdate><enddate>20121204</enddate><creator>Lele, Pushkar P</creator><creator>Branch, Richard W</creator><creator>Nathan, Vedhavalli S. 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| subjects | Bacteria Bacterial Proteins - metabolism Binding sites Biological Sciences Bleaching Chemotaxis Escherichia coli Escherichia coli - chemistry Escherichia coli - physiology Flagella - physiology flagellum Fluorescence Fluorescence Recovery After Photobleaching Membrane Proteins - metabolism Methyl-Accepting Chemotaxis Proteins Microscopy, Fluorescence Models, Chemical Molecular Motor Proteins - metabolism Molecules Motors Physiological regulation Population growth Protein Binding Renovations Rotation |
| title | Mechanism for adaptive remodeling of the bacterial flagellar switch |
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