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Prion Domain Initiation of Amyloid Formation in Vitro from Native Ure2p

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Science  26 Feb 1999:
Vol. 283, Issue 5406, pp. 1339-1343
DOI: 10.1126/science.283.5406.1339

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Abstract

The [URE3] non-Mendelian genetic element of Saccharomyces cerevisiae is an infectious protein (prion) form of Ure2p, a regulator of nitrogen catabolism. Here, synthetic Ure2p1−65 were shown to polymerize to form filaments 40 to 45 angstroms in diameter with more than 60 percent β sheet. Ure2p1−65 specifically induced full-length native Ure2p to copolymerize under conditions where native Ure2p alone did not polymerize. Like Ure2p in extracts of [URE3] strains, these 180- to 220-angstrom-diameter filaments were protease resistant. The Ure2p1−65-Ure2p cofilaments could seed polymerization of native Ure2p to form thicker, less regular filaments. All filaments stained with Congo Red to produce the green birefringence typical of amyloid. This self-propagating amyloid formation can explain the properties of [URE3].

  • * To whom correspondence should be addressed. E-mail: wickner{at}helix.nih.gov

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