研究成果

【代表論文】

分子シャペロン、タンパク質の凝集体形成機構

  • [1] Chadani Y, Niwa T, Chiba S, Taguchi, H.*, Ito K.* Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing. Proc Natl Acad Sci USA. 113, E829-38 (2016)
  • [2] Okuda, M, Niwa, T., *Taguchi, H.* Single-molecule analyses on the dynamics of Hsp104 and protein aggregates. J. Biol. Chem. 290, 7833-7840 (2015)
  • [3] Ishimoto, T., Fujiwara, K., Niwa, T., Taguchi, H.*: Conversion of a chaperonin GroEL-independent protein into an obligate substrate. J. Biol. Chem. 289 32073-32080 (2014)
  • [4] Taguchi, H.* Reaction cycle of chaperonin GroEL via symmetric "football" intermediate (review). J. Mol. Biol. 427, 2912-2918 (2015)
  • [5] Koike-Takeshita, A., Mitsuoka, K., Taguchi, H.* Asp52 in combination with Asp398 plays a critical role in ATP hydrolysis of chaperonin GroEL. J. Biol. Chem. 289 30005-30011 (2014)
  • [6] Niwa, T., Kanamori T., *Ueda, T., *Taguchi, H. Global Analysis of Chaperone Effects Using a Reconstituted Cell-Free Translation System. Proc. Natl. Acad. Sci. U.S.A. 109, 8937-8942 (2012)
  • [7] Fujiwara, K., Ishihama, Y., Nakahigashi, K., Soga, T. and Taguchi, H.* A systematic survey of in vivo obligate chaperonin-dependent substrates. EMBO J. 29, 1552-1564 (2010)
  • [8] Niwa, T., Ying, B.-W., Saito, K., Jin, W. Z., Takada, S., Ueda, T. Taguchi, H.* Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins. Proc. Natl. Acad. Sci. U.S.A. 106, 4201-4206 (2009)
  • [9] #Ueno, T., #Taguchi, H., Tadakuma, H., Yoshida, M., Funatsu, T. GroEL mediates protein folding with a two successive timer mechanism. Mol. Cell 14, 423-434 (2004)
  • [10] Taguchi, H., Ueno, T., Tadakuma, H., Yoshida, M., Funatsu, T. Single-molecule observation of protein-protein interactions in the chaperonin system. Nat. Biotechnol. 19, 861-865 (2001)

酵母プリオン

  • [1] Odani, W, Urata, K, Okuda, M, Okuma, S, Koyama, H, Pack, CG, Fujiwara, K, Nojima, T, Kinjo, M, Kawai-Noma, S, Taguchi, H.* Peptide sequences converting polyglutamine into a prion in yeast. FEBS J. 282, 477-490 (2015)
  • [2] Kawai-Noma, S., Pack, C-G., Kojidani, T., Asakawa, H., Hiraoka, Y., Kinjo, M., Haraguchi, T., Taguchi, H.*, and Hirata, A. In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells. J. Cell Biol. 190, 223-231 (2010)
  • [3] Taguchi, H.* and Kawai-Noma, S. Diffuse oligomer-based transmission of yeast prions. (Review) FEBS J. 277, 1359-1368 (2010)
  • [4] Kawai-Noma, S., Ayano, S., Pack, C-G., Kinjo, M., Yoshida, M., Yasuda, K., Taguchi, H. Dynamics of yeast prion aggregates in single living cells. Genes to Cells 11, 1085-1096 (2006)
  • [5] Inoue, Y., Taguchi, H., Kishimoto, A., Yoshida, M. Hsp104 binds to yeast sup35 prion fiber but needs other factor(s) to sever it. J. Biol. Chem. 279, 52319-52323 (2004)
  • [6] Inoue, Y., Kishimoto, A. et al. Strong growth polarity of yeast prion-fiber revealed by single fiber imaging. J. Biol. Chem. 276, 35227-35230 (2001)

【主な日本語総説】

  • [1] 田口 英樹「タンパク質フォールディングの「理想」と「現実」:凝集形成とシャペロンの役割」生化学 87, 194-204 (2015)
  • [2] 丹羽達也、上田卓也、田口 英樹「大腸菌全タンパク質の凝集性とシャペロン効果の網羅的な解析」生物物理 53, 309-312 (2013)
  • [3] 田口 英樹「タンパク質のフォールディング:理想と現実」高分子 62, 502-504 (2013)

【著書】

  • [1] 「池上彰が聞いてわかった生命のしくみ」池上彰、岩崎博史、田口英樹著、朝日新聞出版、2016年
  • [2] 「学んでみると生命科学はおもしろい」田口英樹著、ベレ出版2014年

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