Structural diversity of bacterial flagellar motors

被引:221
作者
Chen, Songye [1 ]
Beeby, Morgan [1 ,2 ]
Murphy, Gavin E. [1 ]
Leadbetter, Jared R. [3 ]
Hendrixson, David R. [4 ]
Briegel, Ariane [1 ,2 ]
Li, Zhuo [1 ,2 ]
Shi, Jian [1 ,2 ]
Tocheva, Elitza I. [1 ]
Mueller, Axel [5 ]
Dobro, Megan J. [1 ]
Jensen, Grant J. [1 ,2 ]
机构
[1] CALTECH, Div Biol, Pasadena, CA 91125 USA
[2] CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA
[3] CALTECH, Div Environm Sci & Engn, Pasadena, CA 91125 USA
[4] Univ Texas SW Med Ctr Dallas, Dept Microbiol, Dallas, TX 75390 USA
[5] CALTECH, Div Chem, Pasadena, CA 91125 USA
基金
美国国家科学基金会;
关键词
bacterial flagellar motor; electron cryotomography; motility; phylogenetic profiling; subtomogram average; PROTEIN EXPORT APPARATUS; III SECRETION SYSTEM; BASAL BODY; CRYOELECTRON TOMOGRAPHY; SALMONELLA-TYPHIMURIUM; CYTOPLASMIC DOMAIN; ELECTRON CRYOTOMOGRAPHY; CAULOBACTER-CRESCENTUS; MEMBRANE; COMPONENT;
D O I
10.1038/emboj.2011.186
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
The bacterial flagellum is one of nature's most amazing and well-studied nanomachines. Its cell-wall-anchored motor uses chemical energy to rotate a microns-long filament and propel the bacterium towards nutrients and away from toxins. While much is known about flagellar motors from certain model organisms, their diversity across the bacterial kingdom is less well characterized, allowing the occasional misrepresentation of the motor as an invariant, ideal machine. Here, we present an electron cryotomographical survey of flagellar motor architectures throughout the Bacteria. While a conserved structural core was observed in all 11 bacteria imaged, surprisingly novel and divergent structures as well as different symmetries were observed surrounding the core. Correlating the motor structures with the presence and absence of particular motor genes in each organism suggested the locations of five proteins involved in the export apparatus including FliI, whose position below the C-ring was confirmed by imaging a deletion strain. The combination of conserved and specially-adapted structures seen here sheds light on how this complex protein nanomachine has evolved to meet the needs of different species. The EMBO Journal ( 2011) 30, 2972-2981. doi:10.1038/emboj.2011.186; Published online 14 June 2011
引用
收藏
页码:2972 / 2981
页数:10
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