Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S-cerevisiae
Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S-cerevisiae
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DOI：
10.1016/s0092-8674(00)80264-0
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发表时间：
1997-05-30
期刊：
影响因子：
64.5
通讯作者：
Lindquist, S
中科院分区：
文献类型：
--
作者：
Glover, JR;Kowal, AS;Lindquist, S
S.酿酒酵母代表了一种新的遗传形式：改变的表型的胞质传递显然是基于改变的蛋白质结构而不是改变的核酸的遗传。其传播的分子基础是未知的。我们报告，纯化Sup35和亚结构域，诱导[PSI+]元素在体内形成高度有序的纤维在体外。纤维结合刚果红，富含β折叠，这是在某些人类疾病中发现的淀粉样蛋白的特征，包括朊病毒疾病。有些纤维具有独特的结构，这些结构一旦启动，就会自我延续。预成形纤维通过未聚合蛋白质大大促进纤维形成。这些数据支持[PSI+]遗传的“仅蛋白质”接种聚合模型。
The [PSI+] factor of S. cerevisiae represents a new form of inheritance: cytosolic transmission of an altered phenotype is apparently based upon inheritance of an altered protein structure rather than an altered nucleic acid. The molecular basis of its propagation is unknown. We report that purified Sup35 and subdomains that induce [PSI+] elements in vivo form highly ordered fibers in vitro. Fibers bind Congo red and are rich in beta sheet, characteristics of amyloids found in certain human diseases, including the prion diseases. Some fibers have distinct structures and these, once initiated, are self-perpetuating. Preformed fibers greatly accelerate fiber formation by unpolymerized protein. These data support a ''protein-only'' seeded polymerization model for the inheritance of [PSI+].