Patino M M, Liu J J, Glover J R, Lindquist S
Howard Hughes Medical Institute and the Department of Molecular Genetics and Cell Biology, University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA.
Science. 1996 Aug 2;273(5275):622-6. doi: 10.1126/science.273.5275.622.
A cytoplasmically inherited genetic element in yeast, [PSI+], was confirmed to be a prionlike aggregate of the cellular protein Sup35 by differential centrifugation analysis and microscopic localization of a Sup35-green fluorescent protein fusion. Aggregation depended on the intracellular concentration and functional state of the chaperone protein Hsp104 in the same manner as did [PSI+] inheritance. The amino-terminal and carboxy-terminal domains of Sup35 contributed to the unusual behavior of [PSI+]. [PSI+] altered the conformational state of newly synthesized prion proteins, inducing them to aggregate as well, thus fulfilling a major tenet of the prion hypothesis.
酵母中一种细胞质遗传元件[PSI+]，通过差速离心分析和Sup35-绿色荧光蛋白融合体的显微镜定位，被确认为细胞蛋白Sup35的一种类朊病毒聚集体。聚集依赖于伴侣蛋白Hsp104的细胞内浓度和功能状态，其方式与[PSI+]遗传相同。Sup35的氨基末端和羧基末端结构域导致了[PSI+]的异常行为。[PSI+]改变了新合成的朊病毒蛋白的构象状态，也诱导它们聚集，从而符合朊病毒假说的一个主要原则。
