NDLI: Mechanism of inactivation on prion conversion of theSaccharomyces cerevisiae Ure2 protein

Content Provider	PubMed Central
Author	Baxa, Ulrich Speransky, Vladislav Steven, Alasdair C. Wickner, Reed B.
Copyright Year	2002
Abstract	The [URE3] infectious protein (prion) of Saccharomycescerevisiae is a self-propagating amyloid form of Ure2p. TheC-terminal domain of Ure2p controls nitrogen catabolism by complexingwith the transcription factor, Gln3p, whereas the asparagine-richN-terminal “prion” domain is responsible for amyloid filamentformation (prion conversion). On filament formation, Ure2p isinactivated, reflecting either a structural change in the C-terminaldomain or steric blocking of its interaction with Gln3p. We fused theprion domain with four proteins whose activities should not besterically impeded by aggregation because their substrates are verysmall: barnase, carbonic anhydrase, glutathioneS-transferase, and green fluorescent protein. All formedamyloid filaments in vitro, whose diameters increasedwith the mass of the appended enzyme. The helical repeat lengths wereconsistent within a single filament but varied with the construct andbetween filaments from a single construct. CD data suggest that, in thesoluble fusion proteins, the prion domain has no regular secondarystructure, whereas earlier data showed that in filaments, it isvirtually all β-sheet. In filaments, the activity of the appendedproteins was at most mildly reduced, when substrate diffusion effectswere taken into account, indicating that they retained their nativestructures. These observations suggest that the amyloid content ofthese filaments is confined to their prion domain-containing backbonesand imply that Ure2p is inactivated in [URE3] cells by a stericblocking mechanism.
Related Links	http://dx.doi.org/10.1073/pnas.082097899
Ending Page	5260
Page Count	8
Starting Page	5253
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-04-16
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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