Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [ <i>psi</i> <sup>+</sup> ]

  • Yury O. Chernoff
    Department of Biological Sciences, University of Illinois, Chicago, IL 60607-7020, USA.
  • Susan L. Lindquist
    Department of Molecular Genetics and Cell Biology and Howard Hughes Medical Institute, University of Chicago, Chicago, IL 60637, USA.
  • Bun-ichiro Ono
    Faculty of Pharmaceutical Sciences, Okayama University, Okayama 700, Japan.
  • Sergei G. Inge-Vechtomov
    Department of Genetics, St. Petersburg State University, 199034 St. Petersburg, Russia.
  • Susan W. Liebman
    Department of Biological Sciences, University of Illinois, Chicago, IL 60607-7020, USA.

抄録

<jats:p> The yeast non-Mendelian factor [ <jats:italic>psi</jats:italic> <jats:sup>+</jats:sup> ] has been suggested to be a self-modified protein analogous to mammalian prions. Here it is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the [ <jats:italic>psi</jats:italic> <jats:sup>+</jats:sup> ] factor. Overproduction or inactivation of Hsp104 caused the loss of [ <jats:italic>psi</jats:italic> <jats:sup>+</jats:sup> ]. These results suggest that chaperone proteins play a role in prion-like phenomena, and that a certain level of chaperone expression can cure cells of prions without affecting viability. This may lead to antiprion treatments that involve the alteration of chaperone amounts or activity. </jats:p>

収録刊行物

  • Science

    Science 268 (5212), 880-884, 1995-05-12

    American Association for the Advancement of Science (AAAS)

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