In vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion
In vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion
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SpUre2p（一种朊病毒相关蛋白）的体外分析例证了淀粉样蛋白和朊病毒之间的关系
DOI：
10.1074/jbc.m608652200
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发表时间：
2007-03-16
影响因子：
4.8
通讯作者：
Cullin, Christophe
中科院分区：
文献类型：
--
作者：
Immel, Francoise;Jiang, Yi;Cullin, Christophe
酵母酿酒酵母的蛋白质组中含有至少三种朊病毒蛋白。这些蛋白质（Ure2p，Sup35p和Rnq1p）共享一组显着的特性。在体内，它们形成聚集体，使它们的聚集自我延续。这种聚集由Hsp104控制，Hsp104在这些朊病毒的生长和切断中起主要作用。在体外，这些朊病毒蛋白自发形成淀粉样纤维。将由Ure2p或Sup35p制成的这种原纤维引入酵母细胞中分别导致朊病毒表型[URE3]和[PSI]。先前关于酵母朊病毒进化生物学的研究已经清楚地确定，[URE3]在半子囊菌酵母中并不很保守，特别是在S.矛盾的。在这里，我们证明了S。Paradoxus Ure 2p能够形成传染性淀粉样蛋白。这些原纤维比S.酿酒酵母Ure2p原纤维的剪切力。在体内观察到GFP融合体的不同聚集模式证实了SpUre2p形成纤维状结构的更高倾向。我们在体外和体内分析的聚集倾向的S。paradoxus Ure2p提供了一个解释，其感染性的损失，并建议，这种蛋白质属于非朊病毒淀粉样蛋白的世界。
The yeast Saccharomyces cerevisiae contains in its proteome at least three prion proteins. These proteins (Ure2p, Sup35p, and Rnq1p) share a set of remarkable properties. In vivo, they form aggregates that self-perpetuate their aggregation. This aggregation is controlled by Hsp104, which plays a major role in the growth and severing of these prions. In vitro, these prion proteins form amyloid fibrils spontaneously. The introduction of such fibrils made from Ure2p or Sup35p into yeast cells leads to the prion phenotypes [URE3] and [PSI], respectively. Previous studies on evolutionary biology of yeast prions have clearly established that [URE3] is not well conserved in the hemiasco-mycetous yeasts and particularly in S. paradoxus. Here we demonstrated that the S. paradoxus Ure2p is able to form infectious amyloid. These fibrils are more resistant than S. cerevisiae Ure2p fibrils to shear force. The observation, in vivo, of a distinct aggregation pattern for GFP fusions confirms the higher propensity of SpUre2p to form fibrillar structures. Our in vitro and in vivo analysis of aggregation propensity of the S. paradoxus Ure2p provides an explanation for its loss of infective properties and suggests that this protein belongs to the non-prion amyloid world.