期刊
PRION
卷 6, 期 4, 页码 391-399出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/pri.20199
关键词
nucleoporin; nuclear pore complex; yeast prion; GLFG nup; amyloid
资金
- G. Harold and Leila Y. Mathers Charitable Foundation
- NIH [GM061900, GM007520, GM25874, DP5-OD009152-01]
The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that act as genetic elements in an entirely protein-based system of inheritance. The nuclear pore complex (NPC) contains multiple Q/N-rich proteins whose self-assembly has also been proposed to underlie structural and functional properties of the NPC. Here we show that an essential sequence feature of these proteins-repeating GLFG motifs-strongly promotes their self-assembly into amyloids with characteristics of prions. Furthermore, we demonstrate that Nup100 can form bona fide prions, thus establishing a previously undiscovered ability of yeast GLFG nucleoporins to adopt this conformational state in vivo.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据