Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.
Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.
复制标题
[PSI( )] 和 [PIN( )] 酵母朊病毒变体之间的不稳定相互作用。
DOI：
10.1093/genetics/165.4.1675
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发表时间：
2003
期刊：
影响因子：
3.3
通讯作者：
Liebman,SusanW
中科院分区：
文献类型：
--
作者：
Bradley,MichaelE;Liebman,SusanW
酵母Sup35和Rnq1蛋白既可以以非感染性可溶性形式存在，分别为[psi -]或[pin -]，也可以以多种感染性淀粉样蛋白形式存在，称为[psi +]或[pin +]朊病毒变体（或朊病毒株）。先前的研究表明，[PSI+]和[PIN+]朊病毒可以增强彼此的外观。我们发现[PSI+]和[PIN+]的特定朊病毒变体会破坏彼此的稳定遗传。获取[PSI+]通常会阻碍特定[PIN+]变体的继承。相反，一些[PIN+]变体的存在会损害弱[PSI+]变体的遗传，但不会损害强[PSI+]变体的遗传。当Rnq1和绿色荧光蛋白融合表达时，这些相同的[PIN+]变体产生单点荧光模式。另一种[PIN+]变体，形成明显不同的多点荧光模式，不损害[PSI+]遗传。因此，外源朊病毒对朊病毒的破坏取决于所涉及的变异。这些发现可能有助于理解其他淀粉样蛋白形成蛋白之间的相互作用，包括那些与某些人类疾病相关的蛋白。
The yeast Sup35 and Rnq1 proteins can exist in either the noninfectious soluble forms, [psi–]or[pin–], respectively, or the multiple infectious amyloid-like forms called [PSI+]or[PIN+] prion variants (or prion strains). It was previously shown that [PSI+] and [PIN+] prions enhance one another'sde novoappearance. Here we show that specific prion variants of [PSI+] and [PIN+] disrupt each other's stable inheritance. Acquiring [PSI+] often impedes the inheritance of particular [PIN+] variants. Conversely, the presence of some [PIN+] variants impairs the inheritance of weak [PSI+] but not strong [PSI+] variants. These same [PIN+] variants generate a single-dot fluorescence pattern when a fusion of Rnq1 and green fluorescent protein is expressed. Another [PIN+] variant, which forms a distinctly different multiple-dot fluorescence pattern, does not impair [PSI+] inheritance. Thus, destabilization of prions by heterologous prions depends upon the variants involved. These findings may have implications for understanding interactions among other amyloid-forming proteins, including those associated with certain human diseases.