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Prion proteostasis: Hsp104 meets its supporting cast.
Prion ( IF 2.3 ) Pub Date : 2008-10-22 , DOI: 10.4161/pri.2.4.7952
Elizabeth A Sweeny 1 , James Shorter
Affiliation  

Infectious amyloid forms of the release factor, Sup35, comprise the yeast prion [PSI+]. This protein-based unit of inheritance is an evolutionary capacitor able to release cryptic genetic variation during environmental stress and generate potentially beneficial phenotypes. Genetic data have uncovered a sophisticated proteostasis network that tightly regulates [PSI+] formation, propagation and elimination. Central to this network, is the AAA+ ATPase and protein disaggregase, Hsp104. Shifting the balance of the cytosolic Hsp70:Hsp40 chaperone machinery and associated nucleotide exchange factors also influences the [PSI+] prion cycle. Yet, a precise understanding of how these systems co-operate to directly modulate the protein folding events required for sustainable Sup35 prionogenesis has remained elusive. Here, we spotlight recent advances that begin to clarify this issue. We suggest that the Hsp70:Hsp40 chaperone machinery functions collectively as a rheostat that adjusts Hsp104's basic prion-remodeling activities.

中文翻译:

朊病毒蛋白稳态:Hsp104 满足其支持角色。

释放因子 Sup35 的传染性淀粉样蛋白形式包含酵母朊病毒 [PSI+]。这种基于蛋白质的遗传单位是一种进化电容器,能够在环境压力期间释放隐秘的遗传变异并产生潜在的有益表型。遗传数据揭示了一个复杂的蛋白质稳态网络,它严格调节 [PSI+] 的形成、传播和消除。该网络的核心是 AAA+ ATPase 和蛋白质分解酶 Hsp104。改变细胞溶质 Hsp70:Hsp40 分子伴侣机制和相关核苷酸交换因子的平衡也会影响 [PSI+] 朊病毒循环。然而,对这些系统如何合作以直接调节可持续 Sup35 蛋白原发生所需的蛋白质折叠事件的精确理解仍然难以捉摸。这里,我们强调最近开始澄清这个问题的进展。我们建议 Hsp70:Hsp40 分子伴侣机制共同作为调节 Hsp104 的基本朊病毒重塑活动的变阻器。
更新日期:2019-11-01
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