期刊
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY
卷 8, 期 9, 页码 -出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/cshperspect.a023531
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- Intramural Program of the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health
Yeast and fungal prions are infectious proteins, most being self-propagating amyloids of normally soluble proteins. Their effects range from a very mild detriment to lethal, with specific effects dependent on the prion protein and the specific prion variant (prion strain). The prion amyloids of Sup35p, Ure2p, and Rnq1p are in-register, parallel, folded b-sheets, an architecture that naturally suggests a mechanism by which a protein can template its conformation, just as DNA or RNA templates its sequence. Prion propagation is critically affected byan array of chaperone systems, most notably the Hsp104/Hsp70/Hsp40 combination, which is responsible for generating new prion seeds from old filaments. The Btn2/Cur1 antiprion system cures most [URE3] prions that develop, and the Ssb antiprion system blocks [PSI+] generation.
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