Structural differences in the bacterial flagellar motor among bacterial species

作者: Hiroyuki Terashima , Akihiro Kawamoto , Yusuke V. Morimoto , Katsumi Imada , Tohru Minamino

DOI: 10.2142/BIOPHYSICO.14.0_191

关键词:

摘要: The bacterial flagellum is a supramolecular motility machine consisting of the basal body as rotary motor, hook universal joint, and filament helical propeller. Intact structures flagella have been observed for different species by electron cryotomography subtomogram averaging. core C ring, MS rod protein export apparatus, their organization are well conserved, but novel divergent also visualized to surround conserved structure body. This suggests that flagellar motors adapted function in various environments where bacteria live survive. In this review, we will summarize our current findings on motor.

参考文章(57)
C J Jones, M Homma, R M Macnab, Identification of proteins of the outer (L and P) rings of the flagellar basal body of Escherichia coli Journal of Bacteriology. ,vol. 169, pp. 1489- 1492 ,(1987) , 10.1128/JB.169.4.1489-1492.1987
Michio Homma, Kazuhiro Kutsukake, Mitsuyasu Hasebe, Tetsuo Iino, Robert M. Macnab, FlgB, FlgC, FlgF and FlgG: A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium☆ Journal of Molecular Biology. ,vol. 211, pp. 465- 477 ,(1990) , 10.1016/0022-2836(90)90365-S
M Homma, Y Komeda, T Iino, R M Macnab, The flaFIX gene product of Salmonella typhimurium is a flagellar basal body component with a signal peptide for export. Journal of Bacteriology. ,vol. 169, pp. 1493- 1498 ,(1987) , 10.1128/JB.169.4.1493-1498.1987
Ryan Q. Notti, Shibani Bhattacharya, Mirjana Lilic, C. Erec Stebbins, A common assembly module in injectisome and flagellar type III secretion sorting platforms Nature Communications. ,vol. 6, pp. 7125- 7125 ,(2015) , 10.1038/NCOMMS8125
Tohru Minamino, Shinsuke D. J. Yoshimura, Yusuke V. Morimoto, Bertha González-Pedrajo, Nobunori Kami-ike, Keiichi Namba, Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus. Molecular Microbiology. ,vol. 74, pp. 1471- 1483 ,(2009) , 10.1111/J.1365-2958.2009.06946.X
N. Hara, Y. V. Morimoto, A. Kawamoto, K. Namba, T. Minamino, Interaction of the Extreme N-Terminal Region of FliH with FlhA Is Required for Efficient Bacterial Flagellar Protein Export Journal of Bacteriology. ,vol. 194, pp. 5353- 5360 ,(2012) , 10.1128/JB.01028-12
X. Zhao, K. Zhang, T. Boquoi, B. Hu, M. A. Motaleb, K. A. Miller, M. E. James, N. W. Charon, M. D. Manson, S. J. Norris, C. Li, J. Liu, Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi Proceedings of the National Academy of Sciences of the United States of America. ,vol. 110, pp. 14390- 14395 ,(2013) , 10.1073/PNAS.1308306110
T. Akiba, H. Yoshimura, K. Namba, Monolayer crystallization of flagellar L-P rings by sequential addition and depletion of lipid. Science. ,vol. 252, pp. 1544- 1546 ,(1991) , 10.1126/SCIENCE.2047860
Akihiro Kawamoto, Yusuke V. Morimoto, Tomoko Miyata, Tohru Minamino, Kelly T. Hughes, Takayuki Kato, Keiichi Namba, Common and distinct structural features of Salmonella injectisome and flagellar basal body Scientific Reports. ,vol. 3, pp. 3369- 3369 ,(2013) , 10.1038/SREP03369
Tohru Minamino, Yusuke V. Morimoto, Noritaka Hara, Keiichi Namba, An energy transduction mechanism used in bacterial flagellar type III protein export Nature Communications. ,vol. 2, pp. 475- 475 ,(2011) , 10.1038/NCOMMS1488