Prion-Inducing Domain of Yeast Ure2p and Protease Resistance of Ure2p in Prion-Containing Cells
Open Access
- 6 October 1995
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 270 (5233) , 93-95
- https://doi.org/10.1126/science.270.5233.93
Abstract
The genetic properties of the [URE3] non-Mendelian element of Saccharomyces cerevisiae suggest that it is a prion (infectious protein) form of Ure2p, a regulator of nitrogen catabolism. In extracts from [URE3] strains, Ure2p was partially resistant to proteinase K compared with Ure2p from wild-type extracts. Overexpression of Ure2p in wild-type strains induced a 20- to 200-fold increase in the frequency with which [URE3] arose. Overexpression of just the amino-terminal 65 residues of Ure2p increased the frequency of [URE3] induction 6000-fold. Without this “prion-inducing domain” the carboxyl-terminal domain performed the nitrogen regulation function of Ure2p, but could not be changed to the [URE3] prion state. Thus, this domain induced the prion state in trans, whereas in cis it conferred susceptibility of the adjoining nitrogen regulatory domain to prion infections.Keywords
This publication has 27 references indexed in Scilit:
- Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [ psi + ]Science, 1995
- BIOLOGY AND GENETICS OF PRION DISEASESAnnual Review of Microbiology, 1994
- Cytoplasmic Inheritance: Prion-like factors in yeastCurrent Biology, 1994
- Cell-free formation of protease-resistant prion proteinNature, 1994
- Psi no more for yeast prionsNature, 1994
- [URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiaeScience, 1994
- Scrapie prions aggregate to form amyloid-like birefringent rodsCell, 1983
- Identification of a Protein That Purifies with the Scrapie PrionScience, 1982
- Does the Agent of Scrapie Replicate without Nucleic Acid ?Nature, 1967
- Ψ, A cytoplasmic suppressor of super-suppressor in yeastHeredity, 1965