A bipolar functionality of Q/N‐rich proteins: Lsm4 amyloid causes clearance of yeast prions

DOI Web Site Web Site Web Site PubMed 被引用文献1件 参考文献52件 オープンアクセス
  • Keita Oishi
    Department of Basic Medical Sciences Institute of Medical Science University of Tokyo 4‐6‐1 Shirokanedai Minato‐ku Tokyo 108‐8639 Japan
  • Hiroshi Kurahashi
    Department of Basic Medical Sciences Institute of Medical Science University of Tokyo 4‐6‐1 Shirokanedai Minato‐ku Tokyo 108‐8639 Japan
  • Chan‐Gi Pack
    Cellular Informatics Laboratory RIKEN Advanced Science Institute Wako‐shi Saitama 351‐0198 Japan
  • Yasushi Sako
    Cellular Informatics Laboratory RIKEN Advanced Science Institute Wako‐shi Saitama 351‐0198 Japan
  • Yoshikazu Nakamura
    Department of Basic Medical Sciences Institute of Medical Science University of Tokyo 4‐6‐1 Shirokanedai Minato‐ku Tokyo 108‐8639 Japan

説明

<jats:title>Abstract</jats:title><jats:p>Prions are epigenetic modifiers that cause partially loss‐of‐function phenotypes of the proteins in <jats:italic><jats:styled-content style="fixed-case">S</jats:styled-content>accharomyces cerevisiae</jats:italic>. The molecular chaperone network that supports prion propagation in the cell has seen a great progress in the last decade. However, the cellular machinery to activate or deactivate the prion states remains an enigma, largely due to insufficient knowledge of prion‐regulating factors. Here, we report that overexpression of a [<jats:italic>PSI</jats:italic><jats:sup>+</jats:sup>]‐inducible Q/N‐rich protein, Lsm4, eliminates the three major prions [<jats:italic>PSI</jats:italic><jats:sup>+</jats:sup>], [<jats:italic>URE3</jats:italic>], and [<jats:italic>RNQ</jats:italic><jats:sup>+</jats:sup>]. Subcloning analysis revealed that the Q/N‐rich region of Lsm4 is responsible for the prion loss. Lsm4 formed an amyloid in vivo, which seemed to play a crucial role in the prion elimination. Fluorescence correlation spectroscopy analysis revealed that in the course of the Lsm4‐driven [<jats:italic>PSI</jats:italic><jats:sup>+</jats:sup>] elimination, the [<jats:italic>PSI</jats:italic><jats:sup>+</jats:sup>] aggregates undergo a size increase, which ultimately results in the formation of conspicuous foci in otherwise [<jats:italic>psi</jats:italic><jats:sup>−</jats:sup>]‐like mother cells. We also found that the antiprion activity is a general property of [<jats:italic>PSI</jats:italic><jats:sup>+</jats:sup>]‐inducible factors. These data provoked a novel “unified” model that explains both prion induction and elimination by a single scheme.</jats:p>

収録刊行物

被引用文献 (1)*注記

もっと見る

参考文献 (52)*注記

もっと見る

関連プロジェクト

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ