Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure
Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure
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DOI：
10.1073/pnas.0609638103
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发表时间：
2006-12-26
影响因子：
11.1
通讯作者：
Tycko, Robert
中科院分区：
文献类型：
--
作者：
Shewmaker, Frank;Wickner, Reed B.;Tycko, Robert
酿酒酵母的[PSI+]朊病毒是Sup 35 p的自繁殖淀粉样蛋白形式，Sup 35 p是翻译终止因子的亚基。利用固态NMR，我们已经检查了从纯化的重组Sup 35（1-253）体外形成的淀粉样纤维的结构，其由富含谷氨酰胺和天冬酰胺的N-末端123个残基的朊病毒结构域（N）和相邻的130个残基的高电荷M结构域组成。在一系列Sup 35 NM原纤维样品中，C-13-标记在Tyr，Leu或Phe残基的骨架羰基位点或Ala残基的侧链甲基位点，测量C-13核之间的磁偶极-偶极耦合，表明N结构域中几乎所有位点的分子间C-13-C-13距离约为0.5 nm。M结构域中的某些位点也表现出约0.5 nm的分子间距离。这些结果表明，在寄存器中的平行β-片层结构的基础[PSI+]朊病毒现象。
The [PSI+] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Sup35p, a subunit of the translation termination factor. Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35(1-253), consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent 130-residue highly charged M domain. Measurements of magnetic dipole-dipole couplings among C-13 nuclei in a series of Sup35NM fibril samples, C-13-labeled at backbone carbonyl sites of Tyr, Leu, or Phe residues or at side-chain methyl sites of Ala residues, indicate intermolecular C-13-C-13 distances of approximate to 0.5 nm for nearly all sites in the N domain. Certain sites in the M domain also exhibit intermolecular distances of approximate to 0.5 nm. These results indicate that an in-register parallel beta-sheet structure underlies the [PSI+] prion phenomenon.