Papers - WATANABE Yo-hei
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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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Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation. Reviewed
Sugita Saori, Watanabe Kumiko, Hashimoto Kana, Niwa Tatsuya, Uemura Eri, Taguchi Hideki, Watanabe Yo-hei
J Biol Chem. 293 ( 50 ) 19228 - 19239 2018.12
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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
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
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ClpB chaperone passively threads soluble denatured proteins through its central pore Reviewed
Nakazaki Yosuke, Watanabe Yo-hei
Genes to Cells 19 ( 12 ) 891 - 900 2014.12
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Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH Reviewed
Suno R, Shimoyama M, Abe A, Shimamura T, Shimodate N, Watanabe YH, Akiyama Y, Yoshida M
FEBS Lett. 586 ( 19 ) 3117 - 3121 2012.9
Joint Work
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Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein. Reviewed
Mizuno S, Nakazaki Y, Yoshida M, Watanabe YH.
FEBS J. 279 ( 8 ) 1474 - 1484 2012.4
Joint Work
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Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus. Reviewed
Yamasaki T, Nakazaki Y, Yoshida M, Watanabe YH.
FEBS J. 278 ( 13 ) 2395 - 2403 2011.7
Joint Work
Authorship：Lead author
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Temperature-dependent regulation of Thermus thermophilus DnaK/DnaJ chaperones by DafA protein. Reviewed
Mizutani T, Nemoto S, Yoshida M, Watanabe YH.
Genes Cells 14 ( 12 ) 1405 - 1413 2009.12
Joint Work
Authorship：Lead author
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Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity. Reviewed
Watanabe YH, Nakazaki Y, Suno R, Yoshida M.
Biochem. J. 421 ( 1 ) 71 - 77 2009.6
Joint Work
Authorship：Lead author
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ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2. Reviewed
Watanabe YH, Takano M, Yoshida M.
J. Biol. Chem. 280 ( 26 ) 24562 - 24567 2005.7
Joint Work
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Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB. Reviewed
Watanabe YH, Yoshida M.
J. Biol. Chem. 279 ( 16 ) 15723 - 15727 2004.4
Joint Work
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The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Reviewed
Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT.
Cell 115 ( 2 ) 229 - 240 2003.10
Joint Work
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Roles of the two ATP binding sites of ClpB from Thermus thermophilus. Reviewed
Watanabe YH, Motohashi K, Yoshida M.
J. Biol. Chem. 277 ( 8 ) 5804 - 5809 2002.2
Joint Work
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Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin comparison of the H64 mutants. Reviewed
Suzuki T, Watanabe YH, Nagasawa M, Matsuoka A, Shikama K.
Eur. J. Biochem. 267 ( 20 ) 6166 - 6174 2000.10
Joint Work
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Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form. Reviewed
Watanabe YH, Motohashi K, Taguchi H, Yoshida M.
J. Biol. Chem. 275 ( 17 ) 12388 - 12392 2000.4
Joint Work
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Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Reviewed
Motohashi K, Watanabe Y, Yohda M, Yoshida M.
Proc. Natl. Acad. Sci. U. S. A. 96 ( 13 ) 7184 - 7189 1999.6
Joint Work
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African elephant myoglobin with an unusual autoxidation behavior: comparison with the H64Q mutant of sperm whale myoglobin. Reviewed
Tada T, Watanabe YH, Matsuoka A, Ikeda-Saito M, Imai K, Ni-hei Y, Shikama K.
Biochim. Biophys. Acta. 1387 165 - 176 1998.9
Joint Work