what is life, anyway?

From: billwald@juno.com
Date: Wed Aug 09 2000 - 00:21:41 EDT

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    What is life, anyway, and do prions have anything to do with the
    abiogenesis problem?

    billwald@juno.com

    5. MEDICAL BIOLOGY:
    EXPERIMENTAL EVIDENCE SUPPORTING THE PRION HYPOTHESIS
         In general, the "prion hypothesis" postulates that a protein
    (prion), by virtue of its ability to propagate in an altered
    conformation, can act as an infectious agent.
         Prions are apparently infectious agents that lack nucleic
    acid and are composed of a *beta-sheet-rich altered conformation
    of a normal cellular protein. Prion infectivity is believed to
    result from the ability of the prion protein in its altered
    conformation to bind to the normal form of the protein and
    catalyze the conversion of the normal protein to the infectious
    conformation.
         While originally identified as the causative agent for a set
    of related transmissible spongiform encephalopathies, including
    Cruetzfeldt-Jacob disease in humans, scrapie in sheep, and "mad
    cow disease" in cattle, self-propagating beta-sheet-rich protein
    aggregates also underlie a variety of noninfectious
    neurodegenerative diseases. These include the relatively common
    disorders Alzheimer's disease and Parkinson's disease, as well as
    inherited polyglutamine repeat disorders such as Huntington's
    disease. [For more on the above pathologies, see related
    background material below.]
    ... ... H.E. Sparrer et al (4 authors at University of California
    San Francisco, US) report experimental evidence supporting the
    prion hypothesis, the authors making the following points:
         1) In addition to a role in human pathogenesis, beta-sheet-
    rich aggregates of glutamine and asparagine-rich domains mediate
    inheritance of certain prion-like traits ([PSI+] and [URE3]) in
    the yeast Saccharomyces cerevisiae, and the easily manipulated
    genetics of this organism has made yeast prions a rich source of
    information concerning the mechanism of prion propagation in vivo
    as well as the role of prion-based inheritance in the normal
    physiology of a cell.
         2) Starting with purified, bacterially produced protein, the
    authors created a yeast prion-like trait- ([PSI+]) inducing
    agent, the agent based on an altered (prion) conformation of a
    yeast protein (Sup35p). After converting this protein to its
    prion conformation in vitro, the authors introduced it into the
    cytoplasm of living yeast, and this resulted in a greatly
    increased rate of appearance of the well-characterized prion-like
    trait, which is known to result from self-propagating aggregates
    of the altered form of the cellular protein Sup35p [*Note #1].
    The authors state: "Thus, as predicted by the prion hypothesis,
    proteins can act as infectious agents by causing self-propagating
    conformational changes."
         3) In a commentary on the above work, Mick F. Tuite
    (University of Kent Canterbury, UK) states: "[Sparrer et al] show
    that the prion form of the normal yeast protein Sup35p
    effectively seeds a self-propagating conformational change in
    normal Sup35p of living yeast cells. Their demonstration provides
    the finishing touches to an extensive body of data that supports
    the protein-only hypothesis."
    -----------
    H.E. Sparrer et al: Evidence for the prion hypothesis: Induction
    of the yeast [PSI+] factor by in vitro-converted Sup35 protein.
    (Science 28 Jul 00 289:595)
    QY: Jonathan S. Weissman [jsw1@itsa.ucsf.edu]
    -----------
    Mick F. Tuite: Sowing the protein seeds of prion propagation.
    (Science 28 Jul 00 289:556)
    QY: Mick F. Tuite [m.f.tuite@ukc.ac.uk]
    -----------
    Text Notes:
    ... ... *beta-sheet: In general, protein chains fold into
    alpha-helices or beta-sheet structures. The beta-sheet is a
    protein structure where the peptide is extended and stabilized by
    hydrogen bonding between NH and CO groups of different
    polypeptide chains or of separate regions of the same chain.
    ... ... *Note #1: The normal form of the protein Sup35p is
    essential for decoding *messenger RNA (mRNA) in yeast. The normal
    protein is hydrolyzed by *protease and does not aggregate. The
    functionally inactive prion form of Sup35p confers the so-called
    [PSI+] *phenotype on yeast cells. In such strains of yeast,
    Sup35p is found almost exclusively as a protease-resistant, high
    molecular weight-aggregate.
    ... ... *messenger RNA (mRNA): The ribonucleic acid molecule
    transcribed from DNA that carries the coded information
    specifying the sequence of amino acids in a protein.
    ... ... *protease: In general, any enzyme that cleaves proteins,
    usually by hydrolysis.
    ... ... *phenotype: In general, term "phenotype" refers to the
    organism as determined by the interaction between its genetic
    constitution (genotype) and the environment.
    -------------------
    Summary & Notes by SCIENCE-WEEK http://scienceweek.com 11Aug00
    For more information: http://scienceweek.com/swfr.htm
    -------------------
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