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Position |
Professor |
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Research Field |
Life Science / Functional biochemistry, Life Science / Biophysics |
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External Link |
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Graduating School 【 display / non-display 】
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Tohoku University Faculty of Science Graduated
- 1996.3
Graduate School 【 display / non-display 】
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Tokyo Institute of Technology Doctor's Course Completed
- 2001.3
Campus Career 【 display / non-display 】
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KONAN UNIVERSITY Faculty of Science and Engineering Professor
2017.4
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KONAN UNIVERSITY Faculty of Science and Engineering Associate Professor
2013.4 - 2017.3
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KONAN UNIVERSITY Faculty of Science and Engineering Lecturer
2005.4 - 2013.3
External Career 【 display / non-display 】
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東京工業大学資源化学研究所
2004.4 - 2005.3
Country：Japan
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日本学術振興会
2001.4 - 2004.3
Country：Japan
Professional Memberships 【 display / non-display 】
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Protein science society of japan
2014.4
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The biophysical society of japan
2013.4
Papers 【 display / non-display 】
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The fission yeast Greatwall-Endosulfine pathway is required for proper quiescence/G0 phase entry and maintenance. Reviewed
Aono Soma, Haruna Yui, Watanabe Yo-hei, Mochida Satoru, Takeda Kojiro
Genes to Cells 24 ( 2 ) 172 - 186 2019.2
Joint Work
DOI： 10.1111/gtc.12665.
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Sugita Saori, Watanabe Kumiko, Hashimoto Kana, Niwa Tatsuya, Uemura Eri, Taguchi Hideki, Watanabe Yo-hei
293 ( 50 ) 19228 - 19239 2018.12
Joint Work
Authorship：Last author, Corresponding author
ClpB, a bacterial homologue of heat shock protein 104 (Hsp104), can disentangle aggregated proteins with the help of the DnaK, a bacterial Hsp70, and its co-factors. As a member of the expanded superfamily of ATPases associated with diverse cellular activities (AAA+), ClpB forms a hexameric ring structure, with each protomer containing two AAA+ modules, AAA1 and AAA2. A long coiled-coil middle domain (MD) is present in the C-terminal region of the AAA1 and surrounds the main body of the ring. The MD is subdivided into two oppositely directed short coiled-coils, called motif-1 and motif-2. The MD represses the ATPase activity of ClpB, and this repression is reversed by the binding of DnaK to motif-2. To better understand how the MD regulates ClpB activity, here we investigated the roles of motif-1 in ClpB from Thermus thermophilus (TClpB). Using systematic alanine substitution of the conserved charged residues, we identified functionally important residues in motif-1, and using a photoreactive cross-linker and LC-MS/MS analysis, we further explored potential interacting residues. Moreover, we constructed TClpB mutants in which functionally important residues in motif-1 and in other candidate regions were substituted by oppositely charged residues. These analyses revealed that the intra-subunit pair Glu-401-Arg-532 and the inter-subunit pair Asp-404-Arg-180 are functionally important, electrostatically interacting pairs. Considering these structural findings, we conclude that the Glu-401-Arg-532 interaction shifts the equilibrium of the MD conformation to stabilize the activated form and that the Arg-180-Asp-404 interaction contributes to intersubunit signal transduction, essential for ClpB chaperone activities.
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Dynamic structural states of ClpB involved in its disaggregation function. Reviewed
Takayuki Uchihashi, Yo-hei Watanabe, Yosuke Nakazaki, Takashi Yamasaki, Hiroki Watanabe, Takahiro Maruno, Kentaro Ishii, Susumu Uchiyama, Chihong Song, Kazuyoshi Murata, Ryota Iino, Toshio Ando
Nature communications 9 2147 2018.6
Joint Work
Authorship：Lead author, Corresponding author
The ATP-dependent bacterial protein disaggregation machine, ClpB belonging to the AAA+ superfamily, refolds toxic protein aggregates into the native state in cooperation with the cognate Hsp70 partner. The ring-shaped hexamers of ClpB unfold and thread its protein substrate through the central pore. However, their function-related structural dynamics has remained elusive. Here we directly visualize ClpB using high-speed atomic force microscopy (HS-AFM) to gain a mechanistic insight into its disaggregation function. The HS-AFM movies demonstrate massive conformational changes of the hexameric ring during ATP hydrolysis, from a round ring to a spiral and even to a pair of twisted half-spirals. HS-AFM observations of Walker-motif mutants unveil crucial roles of ATP binding and hydrolysis in the oligomer formation and structural dynamics. Furthermore, repressed and hyperactive mutations result in significantly different oligomeric forms. These results provide a comprehensive view for the ATP-driven oligomeric-state transitions that enable ClpB to disentangle protein aggregates.
DOI： 10.1038/s41467-018-04587-w
Other Link： http://www.nature.com/ncomms/
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Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation. Reviewed
Sayaka Hayashi, Yosuke Nakazaki, Kei Kagii, Hiromi Imamura, Yo-hei Watanabe
Scientific Reports 7 ( 1 ) 8648 2017.8
Joint Work
Authorship：Lead author
DOI： 10.1038/s41598-017-08917-8.
Other Link： http://www.nature.com/srep/
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Analysis of the Cooperative ATPase Cycle of the AAA+ Chaperone ClpB from Thermus thermophilus by Using Ordered Heterohexamers with an Alternating Subunit Arrangement Reviewed
Yamasaki Takashi、Oohata Yukiko、Nakamura Toshiki、Watanabe Yo-hei
J Biol Chem. 290 ( 15 ) 9789 - 9800 2015.4
Books and Other Publications 【 display / non-display 】
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ベーシックマスター生化学
西川一八他（ Role： Joint author , 第7章 低分子生理活性物質と金属イオン）
オーム社 2008.11
Review Papers (Misc) 【 display / non-display 】
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リング状ATPaseの新しい反応モデル-しゃくとり虫の動きでDNAを取り込む？
渡辺洋平
蛋白質核酸酵素 54 ( 6 ) 763 - 763 2009.5
Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：共立出版
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Clpプロテアーゼ
渡辺洋平
蛋白質核酸酵素 53 ( 8 ) 1035 - 1036 2008.6
Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：共立出版
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GrpE
渡辺洋平
蛋白質核酸酵素 53 ( 8 ) 1057 - 1057 2008.6
Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：共立出版
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DnaK
渡辺洋平
蛋白質核酸酵素 53 ( 8 ) 1042 - 1042 2008.6
Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：共立出版
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DnaJ
渡辺洋平
蛋白質核酸酵素 53 ( 8 ) 1040 - 1040 2008.6
Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：共立出版
Presentations 【 display / non-display 】
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ATP-dependent structural and functional changes of threonine deaminase from Thermus thermophilus
2023.11
Event date： 2023.11
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Development of a selective proteolytic system using hyperactive ClpB mutant
2023.11
Event date： 2023.11
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Development of novel targeted protein degradation system utilizing ClpB's disaggregation ability
2023.11
Event date： 2023.10 - 2023.11
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Biochemical analysis of threonine deaminase from Thermus thermophilus.
2023.10
Event date： 2023.10 - 2023.11
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Construction of targeted protein degradation system using ClpB disaggregase
2023.7
Event date： 2023.7
Grant-in-Aid for Scientific Research 【 display / non-display 】
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任意のタンパク質やその凝集体を選択的にアンフォールドし分解するシステムの開発
2020.4
JSPS Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research(C)
渡辺洋平