Yo Hei Watanabe

Summary

Affiliation: Konan University
Country: Japan

Publications

  1. doi request reprint Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity
    Yo Hei Watanabe
    Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8 9 1, Kobe 658 8501, Japan
    Biochem J 421:71-7. 2009
  2. doi request reprint Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein
    Sayaka Mizuno
    Department of Biology, Faculty of Science and Engineering, Konan University, Kobe, Japan
    FEBS J 279:1474-84. 2012
  3. doi request reprint Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus
    Takashi Yamasaki
    Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto, Kobe, Japan
    FEBS J 278:2395-403. 2011
  4. doi request reprint Temperature-dependent regulation of Thermus thermophilus DnaK/DnaJ chaperones by DafA protein
    Tadashi Mizutani
    Department of Biology, Faculty of Science and Engineering, Konan University, 8 9 1 Okamoto, Kobe 658 8501, Japan
    Genes Cells 14:1405-13. 2009
  5. doi request reprint ClpB chaperone passively threads soluble denatured proteins through its central pore
    Yosuke Nakazaki
    Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8 9 1, Kobe, 658 8501, Japan Institute for Integrative Neurobiology, Konan University, Okamoto 8 9 1, Kobe, 658 8501, Japan
    Genes Cells 19:891-900. 2014
  6. pmc Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement
    Takashi Yamasaki
    From the Department of Biology, Faculty of Science and Engineering and the Institute for Integrative Neurobiology, Konan University, Okamoto 8 9 1, Kobe 658 8501, Japan
    J Biol Chem 290:9789-800. 2015

Collaborators

  • Masasuke Yoshida
  • Takashi Yamasaki
  • Yosuke Nakazaki
  • Sayaka Mizuno
  • Tadashi Mizutani
  • Toshiki Nakamura
  • Yukiko Oohata
  • Shohei Nemoto

Detail Information

Publications6

  1. doi request reprint Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity
    Yo Hei Watanabe
    Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8 9 1, Kobe 658 8501, Japan
    Biochem J 421:71-7. 2009
    ....
  2. doi request reprint Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein
    Sayaka Mizuno
    Department of Biology, Faculty of Science and Engineering, Konan University, Kobe, Japan
    FEBS J 279:1474-84. 2012
    ..These results indicate that the NTD supports the substrate binding of ClpB and that its conformational shift assists the threading and disaggregation of substrate proteins...
  3. doi request reprint Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus
    Takashi Yamasaki
    Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto, Kobe, Japan
    FEBS J 278:2395-403. 2011
    ..In addition, the two arginines in AAA-1 and the ATP-induced motion of the middle domain independently contribute to the stabilization of the hexamer...
  4. doi request reprint Temperature-dependent regulation of Thermus thermophilus DnaK/DnaJ chaperones by DafA protein
    Tadashi Mizutani
    Department of Biology, Faculty of Science and Engineering, Konan University, 8 9 1 Okamoto, Kobe 658 8501, Japan
    Genes Cells 14:1405-13. 2009
    ..The results indicate that DafA inhibits the chaperone activities of both DnaK and DnaJ by forming the KJA complex and can act as a thermosensor under both heat stress and optimal growth conditions...
  5. doi request reprint ClpB chaperone passively threads soluble denatured proteins through its central pore
    Yosuke Nakazaki
    Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8 9 1, Kobe, 658 8501, Japan Institute for Integrative Neurobiology, Konan University, Okamoto 8 9 1, Kobe, 658 8501, Japan
    Genes Cells 19:891-900. 2014
    ..Moreover, some mutants having no or marginal ATPase activity could thread denatured proteins significantly. These results indicate that ClpB can passively thread soluble denatured proteins...
  6. pmc Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement
    Takashi Yamasaki
    From the Department of Biology, Faculty of Science and Engineering and the Institute for Integrative Neurobiology, Konan University, Okamoto 8 9 1, Kobe 658 8501, Japan
    J Biol Chem 290:9789-800. 2015
    ..We also found that cooperative ATP hydrolysis in at least one ring was needed for the disaggregation activity of ClpB. ..