期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 388, 期 1, 页码 71-84出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.02.004
关键词
bacterial flagellar motor; FliM; FliG; CheY; NMR
资金
- National Institutes of Health [GM 59544]
- University of California Santa Barbara
The high-resolution structures of nearly all the proteins that comprise the bacterial flagellar motor switch complex have been solved; yet a clear picture of the switching mechanism has not emerged. Here, we used NMR to characterize the interaction modes and solution properties of a number of these proteins, including several soluble fragments of the flagellar motor proteins FliM and FliG, and the response-regulator CheY. We find that activated CheY, the switch signal, binds to a previously unidentified region of FliM, adjacent to the FliM-FliM interface. We also find that activated CheY and FliG bind with mutual exclusivity to this site on FliM, because their respective binding surfaces partially overlap. These data support a model of CheY-driven motor switching wherein the binding of activated CheY to FliM displaces the carboxy-terminal domain of FliG (FliG(C)) from FliM, modulating the FliG(C)-MotA interaction, and causing the motor to switch rotational sense as required for chemotaxis. (C) 2009 Elsevier Ltd. All rights reserved.
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