1999 Fiscal Year Final Research Report Summary
STRUCTURAL ANALYSIS OF THE TORQUE GENERATOR IN THE BACTERIAL FLAGELLAR MOTOR
| Project/Area Number |
10480184
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | TEIKYO UNIVERSITY |
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Principal Investigator |
AIZAWA Shin-ichi DEPARTMENT OF BIOSCIENCES, TEIKYO UNIVERSITY, ASSOCIATE PROFESSOR, 理工学部, 助教授 (50222451)
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| Co-Investigator(Kenkyū-buntansha) |
BABA Norio DEPARTMENT OF TECHNOLOGY, KOGAKUIN UNIVERSITY, PROFESSOR, 工学部, 教授 (80164896)
YAMAGUCHI Shigeru DEPARTMENT OF BUSINESS, MEIJI UNIVERSITY, PROFESSOR, 商学部, 教授 (30210363)
KATAYAMA Eisaku INSTITUTE OF MEDICAL SCIENCES, TOKYO UNIVERSITY, ASSOCIATE PROFESSOR, 医科学研究所, 助教授 (50111505)
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| Project Period (FY) |
1998 – 1999
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| Keywords | SALMONELLA / FLAGELLAR MOTOR / TORQUE GENERATOR / QUICK FREEZE METHOD / OSMOTIC SHOCK METHOD / MOT COMPLEX |
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| Research Abstract |
Bacterial flagellar motor rotates by proton motive force, that is, a flow of protons from outside to inside the cell. The main purpose of this project is elucidation of the mechanism of torque generation in the flagellar motor. Especially, we have tried to visualize the torque generator by quick-freeze method using liquid helium. The torque generator has been considered to locate in the periplasmic space, but nobody actually has seen it.
We carried out three experiments during the project term. In short, we could not find any structures related to the torque generator. Under conditions examined, even the C rings were not easily found, probably because of the strains employed. Major technical troubles were to obtain cells cut in half and devoid of DNA and ribosomes.
We also analyzed secreted proteins and found some of the type III dependent secreted proteins were reduced in amount in a mot-deletion mutant. SipA, a major species of them, was turned out to easily get oxidized and make aggregates, indicating that the oxidized conditions on the cell surface may vary in the absence and presence of Mot complexes.
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[Publications] Minamino, T., Gonzalez-Pedrajo, B., Yamaguchi, K., Aizawa, S.-I., and Macnab, R.M.: "FliK the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly"Mol.Microbiol.. 34. 295-304 (1999)
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[Publications] Komoriya, K., Shibano, N., Higano, T., Azuma, N., Yamaguchi, S., and Aizawa, S.-I.: "Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium"Mol.Microbiol.. 34. 767-779 (1999)
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[Publications] Tamano, K., Aizawa, S.-I., Katayama E., Nonaka, T., Imajoh-Ohmi, S., Kuwae, A., Nagai, S., and Sasakawa, C.: "Supramolecular structure of Shigella type III secretion machinery : the needle part is changeable in length and essential for delivery of effectors"EMBO Journal. 19. 3876-3887 (2000)
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[Publications] Shah, D.S.H., Perehine, T., Stevens, S.M., Aizawa, S.-I., and Sockett, E.: "The flagellar filament of R. sphaeroides, pH-induced polymorphic transitions and analysis of the fliC gene"J.Bacteriology. (in press). (2000)
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