Graduate School of Frontier Biosciences, Osaka University


Protonic NanoMachine Group


Original Papers (past 5 years)

  1. Sakai, T., Inoue, Y., Terahara, N., Namba, K. & Minamino, T. (2017) A triangular loop of domain D1 of FlgE is essential for hook assembly but not for the mechanical function. BBRC in press
  2. Terahara, N., Kodera, N., Uchihashi, T., Ando, T., Namba, K. & Minamino, T. (2017) Na+-induced structural transition of MotPS for stator assembly of Bacillus flagellar motor. Science Advances, 3, eaao0419.    
  3. Pourjaberi, S.N.S., Terahara, N., Namba, K. & Minamino, T. (2017) The role of a cytoplasmic loop of MotA in load-dependent assembly and disassembly dynamics of the MotA/B stator complex in the bacterial flagellar motor. Mol. Microbiol. 106, 646-658. 
  4. Takabe, K., Kawamoto, A., Tahara, H., Kudo, S. & Nakamura, S. (2017) Implications of coordinated cell-body rotations for Leptospira motility. BBRC 491, 1040-1046.  
  5. Fukumura, T., Makino, F., Deitsche, T., Kinoshita, M., Kato, T., Wagner, S., Namba, K., Imada, K. & Minamino, T. (2017) Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.  PLOS Biol. 15(8): e2002281(22pp). 
  6. Kinoshita, M., Aizawa, S., Inoue, Y., Namba, K. & Minamino, T. (2017) The role of intrinsically disordered C-terminal region of FliK in substrate specificity switching of the bacterial flagellar type III export apparatus. Mol. Microbiol. 105, 572-588.   
  7. Furukawa, A., Yoshitaie, K., Mori, T., Mori, H., Ito, M., Morimoto, Y.V., Sugano, Y., Iwaki, S., Minamino, T., Sugita, Y., Tanaka, Y. & Tsukazaki, T. (2017) Tunnel formation inferred from the I form structures of the proton-driven protein secretion motor SecDF. Cell Rep. 19: 895-901. 
  8. Hiraoka, K.D., Morimoto, Y.V., Inoue, Y., Fujii, T., Miyata, T., Makino, F., Minamino, T. & Namba, K. (2017) Straight and rigid flagellar hook made by insertion of the FlgG specific sequence into FlgE. Sci. Rep. 7:76723(8pp). 
  9. Terahara, N., Noguchi, Y., Nakamura, S., Kamiike, N., Ito, M., Namba, K., Minamino, T. (2017) Load-and polysaccharide-dependent activation of the Na+-type MotPS stator in the Bacillus subtilis flagellar motor. Sci. Rep. 7:46081(11pp). 
  10. Renault, T.T., Abraham, A.O., Bergmiller, T., Parados, G., Rainville, S., Charpentier, E., Guet, C.C., Tu, Y., Namba, K., Keener, J.P., Minamino, T. & Erhardt, M. (2017) Bacterial flagella grow through an injection-diffusion mechanism. eLife, 6:e23136. 
  11. Fujii, T., Kato, T., Hiraoka, K.D., Miyata, T., Minamino, T., Chevance, F., Hughes, K. & Namba, K. (2017) Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook. Nature Commun. 8:14276 (10pp). 
  12. Fujii, T. & Namba, K. (2017) Structure of actomyosin rigour complex at 5.2Å resolution and insights into the ATPase cycle mechanism. Nature Commun. 8:13969 (11pp).  


  1.  Morimoto, Y.V., Kami-ike, N., Miyata, T., Kawamoto, A., Kato, T., Namba, K. & Minamino, T. (2016) High-resolution pH imaging of living bacterial cell to detect local pH differences. mBio 7(6):e01911-16. 
  2. Makino, F., Shen, D., Kajimura, N., Kawamoto, A., Pissaridou, P., Oswin, H., Pain, M., Murillo, I., Namba, K. & 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. & Minamino, T. (2016) Structural stability of flagellin subunit affects the rate of flagellin export in the absence of FliS chaperone. Mol. Microbiol. 102, 405-416. 
  4. Takekawa, N., Terahara, N., Kato, T., Gohara, M., Mayanagi, K., Hijikata, A., Onoue, Y., Kojima, S., Shirai, T., Namba, K. & Homma, M. (2016) The terameric 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. & Miyata, M. (2016) Structural study of MPN387, an essential protein for gliding motility of a human pathogenic bacterium, Mycoplasma pneumonia. J. Bacteriol. 198, 2352-2359. 
  6. Matsunami, H., Yoon, Y.-H., Meshcheryakov, V.A., Namba, K. & 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. & 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, 656-670. 
  8. Kawamoto, A., Matsuo, L., Kato, T., Yamamoto, H., Namba, K., Miyata, M. (2016) Periodicity in attachment organelle revealed by electron cryotomography suggests conformational changes in gliding mechanism of Mycoplasma pneumoniae. mBio 7(2):e00243-16.   
  9. Baker, M.A.B., Hynson, R.M.G., 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. & Lee, L.K. (2016) Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor. Nature Struct. & Mol. Biol. 23, 197-203.    
  10. Imada, K., Minamino, T., Uchida, Y., Kinoshita, M., 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. USA, 113(13), 3633-3638.  
  11. Minamino, T., Morimoto, Y.V., Hara, N., Aldridge, P.D., 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. 4;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. & Namba, K. (2016) FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella. MicrobiologyOpen, 5(3): 424-435, 2016.    
  13. Komatsu, H., Hayashi, F., Sasa, M., Shikata, K., Yamaguchi, S., Namba, K. & Oosawa, K. (2016) Genetic analysis of revertants isolated from the rod-fragile fliF mutant of Salmonella. Biophys. Physicobiol., 13, 13-25. 

  14. nendai2015.gif
    1. Uchimura, S., Fujii, T., Takazaki, H., Ayukawa, R., Nishikawa, Y., Minoura, I., Hachikubo, Y., Kurisu, G., Sutoh, K., Kon, T., Namba, K., 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. 
    2. McMurry, J.L., Minamino, T., Furukawa, Y., Francis, J.W., Hill, S.A., Helms, K.A., Namba, K. (2015) Weak interactions between Salmonella enterica FlhB and other flagellar export apparatus proteins govern type III secretion dynamics. PLOS One 10, e0134884. 
    3. 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., 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.   
    4. Hanč, P., Fujii, T., Iborra, S., Yamada, Y., Huotari, J., Schulz, O., Ahrens, S., Kjær, S.,   Way, M., Sancho, D., Namba, K., Reis e Sousa, C. (2015) Structures 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, 839-849. 
    5. Nishimura, M., Fujii, T., Hiyoshi, H., Makino, F., Inoue, H., Motooka, D., Kodama, T., Ohkubo, T., Kobayashi, Y., Nakamura, S., Namba K., & 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. 
    6. Iida, T., Mutoh, R., Onai, K., Morishita, M., Furukawa, Y., Namba, K., Ishiura, M. (2015) Importance of the monomer-dimer-tetramer interconversion of the clock protein KaiB in the generation of circadian oscillations in cyanobacteria. Genes to Cells, 20, 173-190.  
    7. 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., Iwaki, K., Namba, K., Komatsu, M., Tanaka, K. & Shirakawa, M. (2015) The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates. Nature Commun. 6:6116.  
    8. Cheung, M., Shen, D.-K., Makino, F., Kato, T., Roehrich, A.D., Martinez-Argudo, I., Walker, M.L., Murillo, L., Liu, X., Pain, M., Brown, J., Frazer, G., Mantell, J., Mina, P., Todd, T., Sessions, R.B., Namba, K. & Blocker, A.J. (2015) Three-dimensional reconstruction from electron microscopy images combined with cysteine-mediated crosslinking provide a model of T3SS needle tip complex. Mol. Microbiol., 95, 31-50.      
    1. Minamino, T., Morimoto, Y.V., Kinoshita, M., Aldridge, P.D., & Namba, K. (2014) The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis. Sci. Rep., 4: 7579. 
    2. Bai, F., Morimoto, Y.V., Yoshimura, S.D.J., Hara, N., Kami-ike, N., Namba, K. & Minamino, T. (2014) Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus. Sci. Rep., 4, 6528. 
    3. Takenaka, T., Endo, M., Suzuki, Y., Yang, Y., Emura, T., Hidaka, K., Kato, T., Miyata, T., Namba, K., Sugiyama, H. (2014) Photoresponsive DNA nanocapsule having an open/close system for capture and release of nanomaterials. Chemistry 20, 1-5. 
    4. Fukumura, T., Furukawa, Y., Kawaguchi, T., Saijo-Hamano, Y., Namba, K., Imada, K. & 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. F70, 1215-1218.  
    5. Nakamura, S., Minamino, T., Kami-ike, N., Kudo, S. & Namba, K. (2014) Effect of the MotB mutation on stator assembly and rotation of the proton-driven bacterial flagellar motor. BIOPHYSICS, 10, 35-41.   
    6. Morimoto, Y.V., Ito, M., Hiraoka, K.D., Che, Y.-S., Bai, F., Kami-ike, N., Namba, K. & Minamino, T. (2014) Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body. Mol. Microbiol., 91, 1214-1226. 
    7. Zhang, S-D., Peterson, N., Zhang, W.-J., Cargou, S., Ruan, J., Murat, D., Santini, C.-L., Song, T., Kato, T., Notareschi, P., Li, Y., Namba, K., Gue, A.-M. & Wu, L.-F. (2014) Swimming behaviour and magnetotaxis function of the marine bacterium strain MO-1. Environmental Microbiology Reports, 6, 14-20.  
    8. Nakamura, S., Leshansky, A., Magariyama, Y., Namba, K. & Kudo, S. (2014) Direct measurement of helical cell motion of the spirochete Leptospira. Biophys. J., 106, 47-54. 
    9. Che, Y.-S., Nakamura, S., Morimoto, Y.V., Kami-ike, N., Namba, K. & Minamino, T. (2014) Load-sensitive coupling of proton translocation and torque generation in the bacterial flagellar motor. Mol. Microbiol., 91, 175-184. 
    1. Castillo, D.J., Nakamura, S., Morimoto, Y.V., Che, Y.-S., Kamiike, N., Kudo, S., Minamino, T. & 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, 9, 173-181.
    2. Kawamoto, A., Morimoto, Y.V., Miyata, T., Minamino, T., Hughes, K.T., Kato, T. & Nambak, K. (2013) Common and distinct structural features of Salmonella infectisome and flagellar basal body. Sci. Rep., 3, 3369. 
    3. Kinoshita, M., Hara, N., Imada, K., Namba, K. & Minamino, T. (2013) Interactions of bacterial flagellar chaperone-substrate complexes with FlhA contribute to coordinating assembly of the flagellar filament. Mol. Microbiol., 90, 1249-1261. 
    4. Woon, A.-P., Tohidpour, A., Alonso, H., Saijo-Hamano, Y., Kwok, T. & Roujeinikova, A. (2013) Conformational analysis of isolated domains of Helicobacter pylori CagA. PLOS One,8, e79367. 
    5. Stadler, A.M., Unruh, T., Namba, K., Samatey, F., Zaccai, G. (2013) Correlation between supercoiling and conformational motions of the bacterial flagellar filament. Biophysical Journal, 105, 2157-2165. 
    6. Bai, F., Che, Y.-S., Kami-ike, N., Ma, Q., Minamino, T., Sowa, Y. & Namba, K. (2013) Populational heterogeneity vs. temporal fluctuation in Esherichia coli flagellar motor switching. Biophysical Journal, 105, 2123-2129. 
    7. Noi, K., Yamamoto, D., Nishikori, S., Arita-Morioka, K., Kato, T., Ando, T., Ogura, T. (2013) High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97. Structure 21, 1-11. 
    8. Watanabe, T.M., Imada, K., Yoshizawa, K., Nishiyama, M., Kato, C., Abe, F., Morikawa, T.J., Kinoshita, M., Fujita, H., Yanagida, T. (2013) Glycine insertion makes yellow fluorescent protein sensitive to hydrostatic pressure. PLOS One, Vol8, e73212. 
    9. Moriya, N., Minamino, T., Ferris, U.H., Morimoto, V.Y., Ashihara, M., Kato, T. and Namba, K. (2013) Role of the Dc domain of the bacterial hook protein FlgE in hook assembly and function. BIOPHYSICS 9, 63-72.
    10. Kishikawa, J., Ibuki, T., Nakamura, S., Nakanishi, A., Minamino, T., Miyata, T., Namba, K., Konno, H., Ueno, H., Imada, K. & Yokoyama, K. (2013) Common evolutionary origin for the rotor domain of rotary ATPases and Flagellar protein export apparatus. PLoS One 8, e64695. 
    11. Gayathri, P., Fujii, T., Namba, K., Lӧwe, J. (2013) Structure of the ParM filament at 8.5Å resolution.Struct. Biol. 184, 33-42. 
    12. Ueta, M., Wada, C., Daifuku, T., Sako, Y., Bessho, Y., Kitamura, A., Ohniwa, R.L., Morikawa, K., Yoshida, H., Kato, T., Miyata, T., Namba, K. & Wada, A. (2013) Conservation of two distinct types of 100S ribosome in bacteria. Genes to Cells 18, 554-574. 
    13. Takei, T., Hasegawa, K., Imada, K., Namba, K., Tsumoto, K., Kuriki, Y., Yoshino, M., Yazaki, K., Kojima, S., Takei, T., Ueda, T., Miura, K.I. (2013) Effects of chain length of an amphipathic polypeptide carrying the repeated amino acid sequence (LETLAKA)(n) on α-helix and fibrous assembly formation. Biochemistry 52, 2810-2820. 
    14. Saijo-Hamano, Y., Matsunami, H., Namba, K. and Imada, K. (2013) Expression, purification, crystallization and preliminary X-ray diffraction analysis of a core fragment of FlgG, a bacterial flagellar rod protein. Acta Cryst., F69, 547-550.  
    15. Takekawa, N., Terauchi, T., Morimoto, Y. V., Minamino, T., Lo, C-J., Kojima, S. & Homma, M. (2013) Na+ conductivity of Na+-driven flagellar motor complex composed of unplugged wild-type or mutant PomB with PomA. J. Biochem. 153, 441-451. 
    16. Cheung, M., Kajimura, N., Makino, F., Ashihara, M., Miyata, T., Kato, T., Namba, K., Blocker, A. J. (2013) A method to achieve homogeneous dispersion of large transmembrane complexes within the holes of carbon films for electron cryomicroscopy. J. Struct. Biol. 182, 51-56. 
    17. Martinez-Argudo, I., Veenendaal, A. K. J., Liu, X., Roehrich, A. D., Roneseen, M. C., Franzoni, G., van Rietschoten, K. N., Morimoto, Y. V., Saijo-Hamano, Y., Avison, M. B., Studholme, D. J., Namba, K., Minamino, T., and Blocker, A. J. (2013) Isolation of Salmonella mutants resistant to the inhibitory effect of salicylidene acylhydrazides on flagella-mediated motility. PLoS One 8, e52179. 
    18. Morimoto, Y.V., Nakamura, S., Hiraoka, K.D., Namba, K., & Minamino, T. (2013) Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation. J. Bacteriol. 195, 474-481. 
    19. Ibuki, T., Uchida, Y., Hironaka, Y., Namba, K., Imada, K., & Minamino, T. (2013) Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus. J. Bacteriol. 195, 466-473. 
    1. Ruan, J., Kato, T., Santini, C.-L., Miyata, T., Kawamoto, A., Zhang, W.-J., Bernadac, A., Wu, L.-F. and Namba, K. (2012) Architecture of a flagellar apparatus in the fast-swimming magnetotactic bacterium MO-1. Proc. Natl. Acad. Sci. USA 109, 20643-20648. 
    2. Gayathri, P., Fujii, T., Møller-Jensen, J., van den Ent, F., Namba, K., Löwe, J. (2012) A bipolar spindle of antiparallel ParM filaments drives bacterial plasmid segregation. Science 338, 1334-1337.
    3. Uchida, Y., Minamino, T., Namba, K. and Imada, K. (2012) Crystallization and preliminary X-ray analysis of the FliH-FliI complex responsible for bacterial flagellar type III protein export. Acta Cryst. F68, 1311-1314.
    4. Monjarás F.J., Garcia-Gómez, E., Espinosa, N., Minamino, T., Namba, K. and González-Pedrajo, B. (2012) Role of EscP in Injectisome Biogenesis and Regulation of Type III Protein Secretion in Enteropathogenic Escherichia coli. J. Bacteriol. 194, 6029-6045.
    5. Terahara, N., Sano, M., Ito, M. (2012) A Bacillus flagellar motor that can use both Na+ and Kas a coupling ion is converted by a single mutation to use only Na+. PLoS One 7, e46248. 
    6. Hara, N., Morimoto, V. Y., Kawamoto, A., Namba, K. & Minamino, T.(2012) Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export. J. Bacteriol. 194, 5353-5360. 
    7. Murakami, R., Mutoh, R., Iwase, R., Furukawa, Y., Imada, K., Onai, K., Morishita, M., Yasui, S., Ishii, K., Valencia, J.S., Uzumaki, T., Namba, K. & Ishiura, M.(2012) The roles of the dimeric and tetrameric structures of the clock protein KaiB in the generation of circadian oscillations in cyanobacteria. J. Biol. Chem. 287, 29506-29515. 

    8. Valencia, S, J, Bitou, K., Ishii, K., Murakami, R., Morishita, M., Onai, K., Furukawa, Y., Imada, K., Namba, K., Ishiura, M. (2012) Phase-dependent generation and transmission of time information by the KaiABC circadian clock oscillator through SasA-KaiC interaction in cyanobacteia. Genes to Cells 17, 398-419. 
    9. Bai, F., Minamino, T., Wu, A., Namba, K. & Xing, J. (2012) Coupling between switching regulation and torque generation in bacterial flagellar motor. Phys. Rev. Lett. 108, 178105. 
    10. Minamino, T., Kinoshita, M., Hara, N., Takeuchi, S., Hida, A., Koya, S., Glenwright, H., Imada, K., Aldridge, P.D., & Namba, K. (2012) Interaction of a flagellar chaperone FlgN with FlhA is required for efficient export of its cognate substrates. Mol. Microbiol. 83, 775-788. 
    11. Fujii, T., Cheung, M., Blanco, A., Kato, T., Blocker, A. J. & Namba, K. (2012) The structure of a type III secretion needle at 7-Å resolution provides insights into its assembly and signaling mechanisms. Proc. Natl. Acad. Sci. USA 109, 4461-4466. 
    12. Matsunami, H., Samatey, F. A., Nagashima, S., Imada, K. & Namba, K. (2012) Crystallization and preliminary X-ray analysis of FlgA, a Periplasmic protein essential for flagellar P-ring assembly. Acta Cryst. F68, 310-313. 
    13. Zhang, W-J., Santini, C-L., Bernadac, A., Ruan, J., Zhang, S-D., Kato, T., Li, Y., Namba, K. & Wu, L-F. (2012) Complex spatial organization and flagellin composition of flagfellar propeller from marine magnetotactic ovoid strain MO-1. J. Mol. Biol. 416, 558-570.  
    14. Stock, D., Namba, K. & Lee, L. K. (2012) Nanorotors and self-assembling macromolecupar machines: the torque ring of the bacterial flagellar motor. Current Opinion in Biotechnology, 23, 1-10. 
    15. Minamino, T., Kinoshita, M., Imada, K. & Namba, K. (2012) Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export. Mol. Microbiol. 83, 168-178. 
    16. Shimada, M., Saijo-Hamano, Y., Furukawa, Y., Minamino, T., Imada, K. & Namba, K. (2012) Functional defect and restoration of temperature-sensitive mutants of FlhA, subunit of the flagellar protein export apparatus. J. Mol. Biol. 415, 855-865. 
    1. Morimoto, Y.V., Minamino, T. (2011) Assembly and activation of the MotA/B proton channel complex of the proton-driven flagellar motor of Salmonella enterica. In Tech.
    2. Minamino, T., Morimoto, Y.V., Hara, N. & Namba, K. (2011) An energy transduction mechanism used in bacterial flagellar type III protein export. Nat. Commun. 2:475.
    3. Aydin, i., Saijo-Hamano, Y., Namba, K., Thomas, C., Roujeinikova, A. (2011) Structural analysis of the essential resuscitation promoting factor YeaZ suggests a mechanism of nucleotide regulation through dimer reorganization. PLoS ONE 6, e23245. 
    4. Hara, N., Namba, K. Minamino, T. (2011) Genetic characterizarion of conserved charged residues in the bacterial flagellar type III export protein FlhA. PLoS ONE 6, e22417. 
    5. Morimoto, Y.V., Kojima, S., Namba, K. & Minamino, T. (2011) M153R mutation in a pH-sensitive green fluorescent protein stabilizes its fusion proteins. PLoS ONE 6, e19598. 
    6. Faulds-Pain, A., Birchall, C., Aldridge, C., Grimaldi, G., Nakamura, S., Miyata, T., Gray J., Li, G., Tang, J., Namba, K., Minamino, T. & Aldridge, P.D. (2011) Flagellin redundancy in Caulobacter 1 crescentus and its implications for flagellar filament assembly. J. Bacteriol. 193, 2695-2707. 
    7. Minamino, T., Imada, K., Kinoshita, M., Nakamura, S., Morimoto, Y.V. & Namba, K. (2011) Structural insight into the rotational switching mechanism of the bacterial flagellar motor. PLoS Biology 9, e1000616. 
    8. Mora, T.,  Bai, F., Che, Y-S., Minamino, T., Namba, K., Wingreen, N.S. (2011) Non-genetic individuality in Escherichia coli motor switching. Phys. Biol. 8, 024001. 
    9. Moriya, N., Minamino, T., Imada, K. & Namba, K. (2011) Genetic analysis of the bacterial hook-capping protein FlgD responsible for hook assembly. Microbiology, 157, 1354-1362. 
    10. Ibuki, T., Imada, K., Minamino, T., Kato, T., Miyata, T. & Namba, K. (2011) Common architecture between the flagellar type III protein export apparatus and F- and V-type ATPases. Nature Struct. & Mo. Biol. 18, 277-282. 
    1. Ju, J., Xu, S., Furukawa, Y., Zhang, Y., Misono, H., Minamino, T., Namba, K.,Zhao, B. & Ohnishi, K. (2010) Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases. J. Biochem. 149, 83-89. 
    2. Aldridge, C., Poonchareon, K., Saini, S., Ewen, T., Soloyva, A., Rao, C.V., Imada, K., Minamino, T. & Aldridge, P.D. (2010) The interaction dynamics of a negative feedback loop regulates flagellar number in Salmonella enterica serovar Typhimurium. Mol. Microbiol. 78, 1416-1430. 
    3. Morimoto, V. Y., Nakamura, S., Kami-ike, N., Namba, K. & Minamino, T. (2010) Charged residues in the cytoplasmic loop of MotA are required for stator assembly into the bacterial flagellar motor. Mol.  Microbiol. 78, 1117-1129. 
    4. Erhardt, M., Namba, K. & Hughes, K.T. (2010) Bacterial nanomachines: The flagellum and Type III injectisome. Cold Spring Harb. Perspect. Biol. 2(11). 
    5. Fujii, T., Iwane, A. H., Yanagida, T. & Namba, K. (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature, 467, 724-729. 
    6. Nakamura, S., Kami-ike, N., Yokota, J. P., Minamino,T. & Namba, K. (2010) Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor. Proc. Natl. Acad. Sci. USA 107, 17616-17620. 
    7. Kato, T., Yoshida, D., Miyata, T., Maki, Y., Wada, A. & Namba, K. (2010) Structure of the 100S ribosome in the hibernation stage revealed by electron cryomicroscopy. Structure, 18, 719-724. 
    8. Imada, K., Minamino, T., Kinoshita, M., Furukawa, Y. & Namba, K. (2010) Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. PNAS, 107, 8812-8817. 
    9. Saijo-Hamano, Y., Imada, K., Minamino, T., Kihara, M., Shimada, M., Kitao,  A. & Namba, K. (2010) Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export. Mol. Microbiol., 76, 260-268
    10. Minamino, T., Shimada, M., Okabe, M., Saijo-Hamano, Y., Imada, K.,  Kihara, M. & Namba, K. (2010) Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export. J. Bacteriol., 197, 1929-1936. 
    11. Maki-Yonekura, S., Yonekura, K. & Namba, K. (2010) Conformational change of flagellin for polymorphic supercoiling of the flagellar filament. Nature Struct. & Mo. Biol.,.17, 417-423. 
    12. Endo, M., Hidaka, K., Kato, T., Namba, K. & Sugiyama, H. (2010) DNA prism structures constructed by folding of multiple rectangular arms. J. Am. Chem. Soc. 131, 15570-15571. 
    13. Yamaguchi, T., Fujii, T., Abe, Y., Hirai, T., Kang, D., Namba, K., Hamasaki, N.  & Mitsuoka, K. (2010) Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals. J. Struct. Biol.., 169, 406-412. 
    14. Morimoto, Y.V., Che, Y., Minamino,T. & Namba, K. (2010) Proton-conductivity assay of plugged and unplugged MotA/B proton channel by cytoplasmic pHluorin expressed in Salmonella. FEBS Letters, 584, 1268-1272.  
    1. Minamino, T., Yoshimura, S.D.J., Morimoto, Y.V., González-Pedrajo, B., Kami-ike, N., Namba, K. (2009)  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. Mol. Microbiol., 74, 1471-1483. 
    2. Fujii, T., Kato, T. & Namba, K. (2009)  Specific arrangement of α-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function. Structure, 17, 1485-1493. 
    3. Minamino, T., Moriya, N., Hirano, T., Hughes, K. T., Namba, K. (2009) Interaction of FliK with the bacterial flagellar hook is required for efficient export specificity switching. Mol. Microbiol. 74, 239-251. 
    4. Nakamura, S., Morimoto, Y.V., Kami-ike, N., Minamino, T. & Namba, K. (2009) Role of a Conserved Prolyl Residue (Pro-173) of MotA in the Mechanochemical Reaction Cycle of the Proton-Driven Flagellar Motor of Salmonella. J. Mol. Biol. 393, 300-307. 
    5. Kazetani, K., Minamino, T., Miyata, T., Kato, T., Namba, K. (2009) ATP-induced FliI hexamerization facilitates bacterial flagellar protein export. Biochemical and Biophysical Research Communications, 388, 323-327. 
    6. Kojima, S., Imada, K., Sakuma, M., Sudo, Y., Kojima, C., Minamino, T., Homma, M. & Namba, K. (2009) Stator assembly and activation mechanism of the flagellar motor by the Periplasmic region of MotB. Mol. Microbiol., Vol. 73, 710-718. 
    7. Kinoshita, M., Yamane, M., Matsunami, H., Minamino, T., Namba,K. & Imada, K.(2009) Purification, crystallization and preliminary X-ray analysis of FliT, a bacterial flagellar substrate-specific export chaperone. Acta Cryst., F65, 825-828. 
    8. Kato, T., Goodman, R.P., Erben, C.M., Turberfield, A.J. & Namba, K. (2009) High-resolution structural analysis of a DNA nanostructure by cryoEM. NANO Letters, Vol.9, No.7, 2747-2750. 
    9. Okabe, M., Minamino, T. , Imada, K., Namba, K. & Kihara, M. (2009) Role of the N-terminal domain of FliI ATPase in bacterial flagellar protein export. FEBS Letters, 583, 743-748. 
    10. Nakamura, S., Kami-ike, N., Yokota, J.P., Kudo, S., Minamino, T., & Namba, K. (2009) Effect of Intracellular pH on the Torque-Speed Relationship of Bacterial Proton-Driven Flagellar Motor. J. Mol. Biol. 386, 332-338. 
    11. Ibuki, T., Shimada, M., Minamino, T., Namba, K. & Imada, K. (2009) Crystallization and preliminary X-ray analysis of FliJ, a cytoplasmic component of the flagellar type III protein export apparatus from Salmonella. Acta Cryst. F65, 47-50. 
    12. Kikuchi, Y. , Matsunami, H., Yamane, M., Imada, K. & Namba, K.(2009) Crystallization and preliminary X-ray analysis of a C-terminal fragment of FlgJ, a putative flagellar rod cap protein of Salmonella. Acta Cryst. F65, 17-20. 

Reviews, Proceedings and Books (past 5 years)

  • Terashima, N., Kawamoto, A., Morimoto, Y.V., Imada, K. & Minamino, T. Structural differences in the bacterial flagellar motor among bacterial species. Biophysics and Physicobiology, in press
  • Morimoto, Y.V., Kami-ike, N., Namba, K. & Minamino, T. (2017) Determination of local pH differences within living Salmonella cells by high-resolution pH imaging based on pH-sensitive GFP derivative, pHluorin(M153R). Bio-protocol 7(1): e2529.
  • Minamino, T., Kinoshita, M., Namba, K. (2017) Fuel of the bacterial flagellar type III protein export apparatus. Methods in Molecular Biology (The Bacterial Flagellum - Methods and Protocols-; Minamino, T., Namba, K. eds.) 1593: p3-16. Humana Press. Springer Nature.  
  • Kawamoto, A., Namba, K. (2017) Structural study of the bacterial flagellar basal body by electron cryomicroscopy and image analysis. Methods in Molecular Biology (The Bacterial Flagellum - Methods and Protocols-; Minamino, T., Namba, K. eds.) 1593: p119-131. Humana Press. Springer Nature. 
  • Morimoto, Y.V., Minamino, T. (2017) Stoichiometry and turnover of the stator and rotor. Methods in Molecular Biology (The Bacterial Flagellum - Methods and Protocols-; Minamino, T., Namba, K. eds.) 1593: p203-213. Humana Press. Springer Nature.  
  • Morimoto, Y.V., Namba, K. & Minamino, T. (2017) Bacterial intracellular sodium ion measurement using CoroNa Green. Bio-protocol 7(1): e2092.
  • Morimoto, Y.V., Namba, K. & Minamino, T. (2017) Measurements of free-swimming speed of motile Salmonella cells in liquid media. Bio-protocol 7(1): e2093.  
  • Minamino T, Imada K. (2015) The bacterial flagellar motor and its structural diversity. Trends in Microbiology, Vol. 23, No.5, 267-274.  
  • Morimoto, V.Y. & Minamino, T. (2014) Structure and function of the bi-directional bacterial flagellar motor. Biomolecules, 4, 217-234.   
  • Minamino, T. (2013) Protein export through the bacterial flagellar type III export pathway. BBA - Molecular Cell Research  for SI: Protein trafficking & Secretion, p1642-1648. 
  • Minamino, T., Kato, T., Miyata, T. & Namba, K. (2013) Electron microscopy of motor structure and possible mechanisms. Encyclopedia of biophysics (Gordon C. K. Roberts, ed.) p591-596, Springer.
  • Kojima, S., Imada, K. & Namba, K. (2010) Stator assembly and activation mechanism of the flagellar motor revealed by the crystal structure of the periplasmic region of MotB. SPring-8 Research Frontiers 2009, 36-37.
  • Joti, Y., Nakasako, M. & Namba, K. (2008) Prospects for Inelastic Neutron Scattering Experiments for Biological Macromolecules. J. Cryst. Soc. Jpn., 50, 78-82.