Education

Ph.D. in Biophysics, Graduate School of Engineering Science, Osaka University, 1980

Current Position

Professor, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan

Publications (since 2014)

1. Morimoto, Y. V., Kami-ike, N., Miyata, T., Kawamoto, A., Kato, T., Namba, K. and Minamino, T. (2016). High-resolution pH imaging of living bacterial cell to detect local pH differences. mBio 7: e01911-16.
   
2. Makino, F., Shen, D., Kajimura, N., Kawamoto, A., Pissaridou, P., Oswin, H., Pain M., Murillo, I., Namba, K. and Blocker, A.J. (2016). The architecture of the cytoplasmic region of type III secretion systems. Sci Rep 6: 33341.
3. Furukawa, Y., Inoue, Y., Sakaguchi, A., Mori, Y., Fukumura, T., Miyata, T., Namba, K. and Minamino, T. (2016). Structural stability of flagellin subunit affects the rate of flagellin export in the absence of FliS chaperone. Mol Microbiol 102(3): 405-416.
4. Takekawa, N., Terahara, N., Kato, T., Gohara, M., Mayanagi, K., Hijikata, A., Onoue, Y., Kojima, S., Shirai, T., Namba, K. and Homma, M. (2016). The tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacterium. Sci Rep 6: 31526.
5. Kawakita, Y., Kinoshita, M., Furukawa, Y., Tulum, I., Tahara, Y. O., Katayama, E., Namba, K. and Miyata, M. (2016). Structural Study of MPN387, an Essential Protein for Gliding Motility of a Human-Pathogenic Bacterium, Mycoplasma pneumoniae. J Bacteriol 198(17): 2352-2359.
6. Matsunami, H., Yoon, Y. H., Meshcheryakov, V. A., Namba, K. and Samatey, F. A. (2016). Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica. Sci Rep 6: 27399.
7. Kinoshita, M., Nakanishi, Y., Furukawa, Y., Namba, K., Imada, K. and Minamino, T. (2016). Rearrangements of alpha-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III export. Mol Microbiol 101(4): 656-670.
8. Kawamoto, A., Matsuo, L., Yamamoto, H., Namba, K. and Miyata, M. (2016). Periodicity in attachment organelle revealed by electron cryotomography suggests conformational changes in gliding mechanism of Mycoplasma pneumoniae. mBio 7: e00243-16.
9. Baker, M. A., Hynson, R. M., Ganuelas, L. A., Mohammadi, N. S., Liew, C. W., Rey, A. A., Duff, A. P., Whitten, A. E., Jeffries, C. M., Delalez, N. J., Morimoto, Y. V., Stock, D., Armitage, J. P., Turberfield, A. J., Namba, K., Berry, R. M. and Lee, L. K. (2016). Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor. Nat Struct Mol Biol 23(3): 197-203.
10. Imada, K., Minamino, T., Uchida, Y., Kinoshita, M. and Namba, K. (2016). Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator. Proc Natl Acad Sci U S A 113(13): 3633-3638.
11. Minamino, T., Morimoto, Y. V., Hara, N., Aldridge, P. D. and Namba, K. (2016). The Bacterial Flagellar Type III Export Gate Complex Is a Dual Fuel Engine That Can Use Both H+ and Na+ for Flagellar Protein Export. PLoS Pathog 12(3): e1005495.
12. Minamino, T., Kinoshita, M., Inoue, Y., Morimoto, Y. V., Ihara, K., Koya, S., Hara, N., Nishioka, N., Kojima, S., Homma, M. and Namba, K. (2016). FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella. Microbiologyopen 5(3): 424-435.
13. Komatsu, H., Hayashi, F., Sasa, M., Shikata, K., Yamaguchi, S., Namba, K. and Oosawa, K. (2016). Genetic analysis of revertants isolated from the rod-fragile fliF mutant of Salmonella. Biophys Physicobiol 13: 13-25.
14. Uchimura, S., Fujii, T., Takazaki, H., Ayukawa, R., Nishikawa, Y., Minoura, I., Hachikubo, Y., Kurisu, G., Sutoh, K., Kon, T., Namba, K. and Muto, E. (2015). A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation. J Cell Biol 208: 211-222.
15. McMurry, J. L., Minamino, T., Furukawa, Y., Francis, J. W., Hill, S. A., Helms, K. A. and Namba, K. (2015). Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics. PLoS One 10(8): e0134884.
16. Oroguchi, T., Sekiguchi, Y., Kobayashi, A., Masaki, Y., Fukuda, A., Hashimoto, S., Nakasako, M., Ichikawa, Y., Kurumizaka, H., Shimizu, M., Inui, Y., Matsunaga, S., Kato, T., Namba, K., Yamaguchi, K., Kuwata, K., Kameda, H., Fukui, N., Kawata, Y., Kameshima, T., Takayama, Y., Yonekura, K. and Yamamoto, M. (2015). Cryogenic coherent X-ray diffraction imaging for biological non-crystalline particles using the KOTOBUKI-1 diffraction apparatus at SACLA. J Phys B: At Mol Opt Phys 48: 184003.
    
17. Nishimura, M., Fujii, T., Hiyoshi, H., Makino, F., Inoue, H., Motooka, D., Kodama, T., Ohkubo, T., Kobayashi, Y., Nakamura, S., Namba K., and Iida, T. (2015). A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments. Sci Rep 5: 10870.
18. Hanc, P., Fujii, T., Iborra, S., Yamada, Y., Huotari, J., Schulz, O., Ahrens, S., Kjaer, S., Way, M., Sancho, D., Namba, K. and Reis e Sousa, C. (2015). Structure of the Complex of F-Actin and DNGR-1, a C-Type Lectin Receptor Involved in Dendritic Cell Cross-Presentation of Dead Cell-Associated Antigens. Immunity 42(5): 839-849.
19. Iida, T., Mutoh, R., Onai, K., Morishita, M., Furukawa, Y., Namba, K. and Ishiura, M. (2015). Importance of the monomer-dimer-tetramer interconversion of the clock protein KaiB in the generation of circadian oscillations in cyanobacteria. Genes Cells 20(3): 173-190.
20. Morimoto, D., Walinda, E., Fukada, H., Sou, Y. S., Kageyama, S., Hoshino, M., Fujii, T., Tsuchiya, H., Saeki, Y., Arita, K., Ariyoshi, M., Tochio, H., Iwai, K., Namba, K., Komatsu, M., Tanaka, K. and Shirakawa, M. (2015). The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates. Nat Commun 6: 6116.
21. Furukawa, Y., Teraguchi, S., Ikegami, T., Dagliyan, O., Jin, L., Hall, D., Dokholyan, N. V., Namba, K., Akira, S., Kurosaki, T., Baba, Y. and Standley, D. M. (2014). Intrinsic disorder mediates cooperative signal transduction in STIM1. J Mol Biol 426(10): 2082-2097.
22. Cheung, M., Shen, D. K., Makino, F., Kato, T., Roehrich, A. D., Martinez-Argudo, I., Walker, M. L., Murillo, I., Liu, X., Pain, M., Brown, J., Frazer, G., Mantell, J., Mina, P., Todd, T., Sessions, R. B., Namba, K. and Blocker, A. J. (2015). Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex. Mol Microbiol 95(1): 31-50.
23. Minamino, T., Morimoto, Y. V., Kinoshita, M., Aldridge, P. D. and Namba, K. (2014). The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis. Sci Rep 4: 7579.
24. Bai, F., Morimoto, Y. V., Yoshimura, S. D. J., Hara, N., Kami-ike, N., Namba, K. and Minamino, T. (2014). Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus. Sci Rep 4: 6528.
25. Takenaka, T., Endo, M., Suzuki, Y., Yang, Y., Emura, T., Hidaka, K., Kato, T., Miyata, T., Namba, K. and Sugiyama, H. (2014). Photoresponsive DNA nanocapsule having an open/close system for capture and release of nanomaterials. Chemistry 20(46): 14951-14954.
26. Fukumura, T., Furukawa, Y., Kawaguchi, T., Saijo-Hamano, Y., Namba, K., Imada, K. and Minamino, T. (2014). Crystallization and preliminary X-ray analysis of the periplasmic domain of FliP, an integral membrane component of the bacterial flagellar type III protein-export apparatus. Acta Crystallogr F Struct Biol Commun 70(Pt 9): 1215-1218.
27. Nakamura, S., Minamino, T., Kami-Ike, N., Kudo, S. and Namba, K. (2014). Effect of the MotB(D33N) mutation on stator assembly and rotation of the proton-driven bacterial flagellar motor. Biophysics (Nagoya-shi) 10: 35-41.
28. Morimoto, Y. V., Ito, M., Hiraoka, K. D., Che, Y. S., Bai, F., Kami-Ike, N., Namba, K. and Minamino, T. (2014). Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body. Mol Microbiol 91(6): 1214-1226.
29. Castillo, D. J., Nakamura, S., Morimoto, Y. V., Che, Y. S., Kami-Ike, N., Kudo, S., Minamino, T. and Namba, K. (2013). The C-terminal periplasmic domain of MotB is responsible for load-dependent control of the number of stators of the bacterial flagellar motor. Biophysics (Nagoya-shi) 9: 173-181.
30. Nakamura, S., Leshansky, A., Magariyama, Y., Namba, K. and Kudo, S. (2014). Direct measurement of helical cell motion of the spirochete leptospira. Biophys J 106(1): 47-54.