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Review
Prion Stability
Brian S. Cox, Lee Byrne and Mick F. Tuite
volume 1 | issue 3
july/august/september 2007Pages: 170 - 178
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The rate of spontaneous change from y- to the y+ condition determined in yeast by states of the Sup35p protein is briefly discussed, together with the conditions necessary for such change to occur. Conditions that promote and which affect the rate of induction of y+ in Sup35p and of other prion-forming proteins to their respective prion forms are also discussed. These include the influence of the amount of nonprion protein, the presence of other prions, the activity of chaperones, and brief descriptions of the role of native sequences in the proteins and how alteration of sequences in prion-forming proteins influence the rate of induction of [prion+] and amyloid forms. The second part of this article discusses the conditions which affect the reversion of y+ to y-, including factors which affect the copy-number of prion “seeds” or propagons and their partition. The principal factor discussed is the activity of the chaperone Hsp104, but the existence of other factors, such a protein sequence and of other, less well-studied agents, is touched upon and comparisons are made, as appropriate, with studies with other yeast prions. We conclude with a discussion of models of maintenance, in particular that of Tanaka et al recently published in Nature (2006),6 which provides much insight into the phenotypic and genetic parameters of the numerous “variants” of prions increasingly being described in the literature.
Authors
Brian S. Cox
Lee Byrne
Research School of Biological Sciences, University of Kent
Mick F. Tuite
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.