Prion Domain Initiation of Amyloid Formation in Vitro from Native Ure2p
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 Ure2p 1−65 were shown to polymerize to form filaments 40 to 45 angstroms in diameter with more than 60 percent β sheet. Ure2p 1−65 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 Ure2p 1−65 -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].
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Feb 26, 1999
- Source ID
- 10.1126/science.283.5406.1339
Entities
People
- Alasdair C. Steven
- Kimberly L. Taylor
- Naiqian Cheng
- Reed B. Wickner
- Robert W. Williams
Organizations
- National Institute of Arthritis and Musculoskeletal and Skin Diseases
- National Institute of Diabetes and Digestive and Kidney Diseases