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Reference: Loovers HM, et al. (2007) Importance of the hsp70 ATPase domain in yeast prion propagation. Genetics 175(2):621-30

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Abstract

The Saccharomyces cerevisiae non-mendelian genetic element [PSI+] is the prion form of the translation termination factor Sup35p. The ability of [PSI+] to propagate efficiently has been shown previously to depend upon the action of protein chaperones. In this paper we describe a genetic screen that identifies an array of mutants within the two major cytosolic Hsp70 chaperones of yeast, Ssa1p and Ssa2p, which impair the propagation of [PSI+]. All but one of the mutants was located within the ATPase domain of Hsp70 which highlights the important role of regulation of Hsp70-Ssa ATP hydrolysis in prion propagation. A subset of mutants are shown to alter Hsp70 function in a way that is distinct from previously characterized Hsp70 mutants that alter [PSI+] propagation, and support the importance of inter-domain communication and Hsp70 interaction with nucleotide exchange factors in prion propagation. Analysis of the effects of Hsp70 mutants upon propagation of a second yeast prion [URE3] further classifies these mutants as having general or prion-specific inhibitory properties.

Reference Type
Journal Article
Authors
Loovers HM, Guinan E, Jones GW
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