The same but different: the role of Hsp70 in heat shock response and prion propagation
The same but different: the role of Hsp70 in heat shock response and prion propagation
复制标题
相同但不同：Hsp70 在热休克反应和朊病毒传播中的作用
DOI：
10.1080/19336896.2018.1507579
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发表时间：
2018
期刊：
影响因子：
2.3
通讯作者：
Jones Gary W.
中科院分区：
文献类型：
--
作者：
Xu Linan;Gong Weibin;Zhang Hong;Perrett Sarah;Jones Gary W.
摘要Hsp70分子伴侣机制是酵母热休克反应的关键组成部分，也是Pron繁殖的调节器。优化Hsp70功能的一个主要因素是蛋白质的核苷酸结合域和底物结合域的高度协调活性。HSP70通过两个结构域之间的双向变构相互作用网络进行域间通信。最近的研究发现，底物结合区的β6/β7区域在优化热休克蛋白70的应激反应和蛋白传播功能方面起着关键作用，并强调了结构域之间的变构相互作用界面。重要的是，虽然Hsp70的功能变化可以导致应激反应和普恩病毒传播的表型后果，但这些变化非法的表型影响水平可能存在显著差异。
ABSTRACT The Hsp70 chaperone machinery is a key component of the heat-shock response and a modulator of prion propagation in yeast. A major factor in optimizing Hsp70 function is the highly coordinated activities of the nucleotide-binding and substrate-binding domains of the protein. Hsp70 inter-domain communication occurs through a bidirectional allosteric interaction network between the two domains. Recent findings identified the β6/β7 region of the substrate-binding domain as playing a critical role in optimizing Hsp70 function in both the stress response and prion propagation and highlighted the allosteric interaction interface between the domains. Importantly, while functional changes in Hsp70 can result in phenotypic consequences for both the stress response and prion propagation, there can be significant differences in the levels of phenotypic impact that such changes illicit.