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)
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.