Molecular Chaperones and the Proteosome : the Mechanism of Controlling the Protein Synthesis and Degradation (The Seminar, "Stresses and Responses and Adaptation of Living Organisms : Molecular and Cellular Mechanisms and its Application")

DOI Web Site 3 References
  • MINAMI Yasufumi
    UPBSB and Department of Biochemistry and Biophysics, School of Science, The University of Tokyo

Bibliographic Information

Other Title
  • 分子シャペロンとプロテアソーム : タンパク質の生成と分解をコントロールする仕組み(セミナー「ストレスと生物の応答・適応 : その分子・細胞機構と応用」)
  • 分子シャペロンとプロテアソーム--タンパク質の生成と分解をコントロールする仕組み
  • ブンシ シャペロン ト プロテアソーム タンパクシツ ノ セイセイ ト ブンカイ オ コントロール スル シクミ

Search this article

Description

We have shown that the 90-kDa heat shock protein (Hsp90) is able to bind partially unfolded firefly luciferase and maintain it in a refoldable state, and that the subsequent successive action of the 20S proteasome activator, PA28, Hsc70 and Hsp40 enables the refolding of the unfolded luciferase. It is most plausible that both the N- and C-terminal chaperone sites of Hsp90 participate in this protein refolding pathway.

Journal

References(3)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top