The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Prion-Inducing Domain of Yeast Ure2p and Protease Resistance of Ure2p in Prion-Containing Cells
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.
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Prions Affect the Appearance of Other Prions
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Prions as adaptive conduits of memory and inheritance
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Emerging Principles of Conformation-Based Prion Inheritance
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Metadata
- Authors
- Masison, D. C., & Wickner, R. B.
- Venue
- Science
- Published
- 1995-10-06
- Volume
- 270
- Issue
- 5233
- Pages
- 93-95
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2032015542
- Cited by
- 347
- References
- 22
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- closed
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- Masison, D. C., & Wickner, R. B. (1995). Prion-Inducing Domain of Yeast Ure2p and Protease Resistance of Ure2p in Prion-Containing Cells. Science. https://doi.org/10.1126/science.270.5233.93
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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