Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies
Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies
复制标题
体现独特酵母朊病毒表型的淀粉样原纤维表现出不同的形态
作者：
Rupam Ghosh;Jijun Dong;Joe Wall;K. K. Frederick
摘要酵母朊病毒是一种以蛋白质为模板的自模板遗传机制，其构象变化导致获得多种新的表型。其中研究得最好的是Sup35的朊病毒结构域（NM），其形成淀粉样蛋白，当引入不携带朊病毒的细胞中时，淀粉样蛋白可以采用几种不同的构象（菌株），从而赋予不同的表型。在这里，我们调查的结构NM纤维模板与细胞裂解物的朊病毒构象。我们的电子显微镜研究表明，NM原纤维，赋予强或弱朊病毒表型都是薄和厚的原纤维，导致包装的M域的差异的混合物。强NM原纤维具有更多的细原纤维，弱NM原纤维具有更多的粗原纤维。有趣的是，单位长度的质量和固态NMR都揭示了薄和厚的原纤维在朊病毒菌株变体中具有不同的基本分子结构，这些结构不相互转化。
ABSTRACT Yeast prions are self‐templating protein‐based mechanisms of inheritance whose conformational changes lead to the acquisition of diverse new phenotypes. The best studied of these is the prion domain (NM) of Sup35, which forms an amyloid that can adopt several distinct conformations (strains) that confer distinct phenotypes when introduced into cells that do not carry the prion. Here, we investigate the structure of NM fibrils templated into the prion conformation with cellular lysates. Our electron microscopy studies reveal that NM fibrils that confer either a strong or a weak prion phenotype are both mixtures of thin and thick fibrils that result from differences in packing of the M domain. Strong NM fibrils have more thin fibrils and weak NM fibrils have more thick fibrils. Interestingly, both mass per length and solid state NMR reveal that the thin and thick fibrils have different underlying molecular structures in the prion strain variants that do not interconvert.
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影响因子：
56.9
作者：
Franzmann, Titus M.;Jahnel, Marcus;Alberti, Simon
通讯作者：
Alberti, Simon
酵母朊病毒 [psi ] 及其决定簇 Sup35p。
影响因子：
--
作者：
Serio,TR;Cashikar,AG;Moslehi,JJ;Kowal,AS;Lindquist,SL
通讯作者：
Lindquist,SL
影响因子：
2.9
作者：
Shewmaker, Frank;Kryndushkin, Dmitry;Chen, Bo;Tycko, Robert;Wickner, Reed B.
通讯作者：
Wickner, Reed B.
影响因子：
15
作者：
Jaroniec, CP;Filip, C;Griffin, RG
通讯作者：
Griffin, RG