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Chapter category: Protein

Prion Stability

This chapter appears in the following book:

Protein-Based Inheritance

Edited by: Yury O. Chernoff
ISBN: 978-1-58706-138-7
» Get more information about this book at landesbioscience.com «

Chapter authors:
Brian S. Cox, Lee Byrne and Mick F. Tuite

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.

Brian S. Cox
University of Kent

Lee Byrne

Mick F. Tuite
University of Kent

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Additional chapters from this book:

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Prion Stability

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