Jones, G.W. and Tuite, M.F. (2005) Chaperoning prions: the cellular machinery for propagating an infectious protein? Bioessays, 27 (8). pp. 823-832. ISSN 0265-9247 .
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Newly made polypeptide chains require the help of molecular chaperones not only to rapidly reach their final three-dimensional forms, but also to unfold and then correctly refold them back to their biologically active form should they misfold. Most prions are an unusual type of protein that can exist in one of two stable conformations, one of which leads to formation of an infectious alternatively folded form. Studies in Baker's yeast (Saccharomyces cerevisiae) have revealed that prions can exploit the molecular chaperone machinery in the cell in order to ensure stable propagation of the infectious, aggregation-prone form. The disaggregation of yeast prion aggregates by molecular chaperones generates forms of the prion protein that can seed the protein polymerisation that underlies the prion propagation cycle. In this article, we review what we have learnt about the role of molecular chaperones in yeast prion propagation, describe a model that can explain the role of various classes of molecular chaperones and their co-chaperones, and speculate on the possible involvement of chaperones in the propagation of mammalian prions.
|Additional information:||0265-9247 (Print) Journal Article Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Review|
|Uncontrolled keywords:||Cytosol/metabolism Fungal Proteins/chemistry Green Fluorescent Proteins/metabolism HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins/metabolism Heat-Shock Proteins/metabolism Macromolecular Substances/chemistry Models, Biological Molecular Chaperones/chemistry/metabolism Peptides/chemistry Prions/chemistry/*physiology Protein Denaturation Protein Folding Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins/metabolism|
|Subjects:||Q Science > QR Microbiology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Mick Tuite|
|Date Deposited:||04 Sep 2008 17:07|
|Last Modified:||14 Jan 2010 14:20|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/5477 (The current URI for this page, for reference purposes)|
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