Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S-cerevisiae

被引：543

作者：

Glover, JR ^{[1
]}

Kowal, AS ^{[1
]}

Schirmer, EC ^{[1
]}

Patino, MM ^{[1
]}

Liu, JJ ^{[1
]}

Lindquist, S ^{[1
]}

机构：

[1] UNIV CHICAGO, HOWARD HUGHES MED INST, DEPT MOL GENET & CELL BIOL, CHICAGO, IL 60637 USA

来源：

CELL | 1997年 / 89卷 / 05期

关键词：

YEAST SACCHAROMYCES-CEREVISIAE; ALZHEIMERS-DISEASE; AMYLOID FORMATION; GENE; SCRAPIE; TERMINATION; PROPAGATION; TRANSLATION; EXPRESSION; VECTORS;

D O I：

10.1016/S0092-8674(00)80264-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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+].

引用

页码：811 / 819

页数：9

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