Specificity of Prion Assembly in Vivo

Specificity of Prion Assembly in Vivo
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体内朊病毒组装的特异性

DOI:
--
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发表时间:
2004
影响因子:
4.8
通讯作者:
S. Liebman
S. Liebman
中科院分区:
生物学2区
文献类型:
--
作者:
Sviatoslav N. Bagriantsev;S. Liebman

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酵母[PSI+]和[PIN+]分别是富含Gln/Asn的蛋白质Sup35p和Rnq1p的自繁殖淀粉样聚集体。和哺乳动物PrP蛋白一样,[PSI+]和[PIN+]以不同的构象存在,称为变异体。在这里,[PSI+]和[PIN+]变体被用来模拟共存的异种淀粉样聚集体之间的体内相互作用。对于[PIN+],演示了两个层次的结构组织,就像前面描述的[PSI+]。在同时含有[PSI+]和[PIN+]的细胞中,两个Prion在两个水平上形成了独立的结构。此外,某些[PIN+]变体导致的[PSI+]不稳定并不涉及[PSI+]普里子大小的改变。最后,当具有不同生物化学特性的聚集体的同一普恩的两个变种组合在一个细胞中时,只有一种聚集体类型被繁殖。这些研究证明了酵母蛋白的细胞内组织,并提供了对体内淀粉样蛋白组装原理的洞察。
The yeast prions [PSI+] and [PIN+] are self-propagating amyloid aggregates of the Gln/Asn-rich proteins Sup35p and Rnq1p, respectively. Like the mammalian PrP prion “strains,” [PSI+] and [PIN+] exist in different conformations called variants. Here, [PSI+] and [PIN+] variants were used to model in vivo interactions between co-existing heterologous amyloid aggregates. Two levels of structural organization, like those previously described for [PSI+], were demonstrated for [PIN+]. In cells with both [PSI+] and [PIN+] the two prions formed separate structures at both levels. Also, the destabilization of [PSI+] by certain [PIN+] variants was shown not to involve alterations in the [PSI+] prion size. Finally, when two variants of the same prion that have aggregates with distinct biochemical characteristics were combined in a single cell, only one aggregate type was propagated. These studies demonstrate the intracellular organization of yeast prions and provide insight into the principles of in vivo amyloid assembly.
DOI: --
发表时间: 1996-12
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影响因子: --
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