Motility protein complexes in the bacterial flagellar motor

被引:108
作者
Tang, H
Braun, TF
Blair, DF
机构
[1] Department of Biology, University of Utah, Salt Lake City
关键词
flagella; energy transduction; mechanoenzyme; protein interactions;
D O I
10.1006/jmbi.1996.0453
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Among the many proteins needed for the assembly and function of bacterial flagella, only five have been suggested to be involved in torque generation. These are MotA, MotB, FliG, FliM and FliN. In this study, we have probed binding interactions among these proteins, by using protein fusions to glutathione S-transferase or to oligo-histidine, in conjunction with co-isolation assays. The results show that FliG, FliM and FliN all bind to each other, and that each also self-associates. MotA and MotB also bind to each other, and MotA interacts, but only weakly, with FliG and FliM. Taken together with previous genetic, physiological and ultrastructural studies, these results provide strong support for the view that FliG, FliM and FliN function together in a complex on the rotor of the flagellar motor, whereas MotA and MotB form a distinct complex that functions as the stator. Torque generation in the flagellar motor is thus likely to involve interactions between these two protein complexes. (C) 1996 Academic Press Limited
引用
收藏
页码:209 / 221
页数:13
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