The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation
The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation
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DOI：
10.1016/j.jmb.2004.03.033
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发表时间：
2004-05-28
影响因子：
5.6
通讯作者：
Steven, AC
中科院分区：
文献类型：
--
作者：
Baxa, U;Ross, PD;Steven, AC
根据Ure 2 p朊病毒发生的“淀粉样蛋白骨架”模型，Ure 2 p的N-末端结构域聚合形成被C-末端结构域包围的淀粉样蛋白丝骨架。后者结构域保留其天然谷胱甘肽-S-转移酶（GST）样折叠，但在氮催化剂中的调节作用空间失活。我们已经测试了这个模型的可溶性和丝状Ure 2 p和可溶性C-末端结构域的差示扫描量热法，结合电子显微镜。正如预测的那样，C-末端结构域在所有三种状态下对热扰动的响应相同，在76 ℃下表现出单一的吸热。相比之下，没有热信号与N-末端结构域相关：在可溶状态的Ure 2 p中，因为它们是未折叠的;在丝状状态，因为它们坚固的淀粉样蛋白构象抵抗加热到100 ℃。爱思唯尔有限公司出版
According to the "amyloid backbone" model of Ure2p prionogenesis, the N-terminal domain of Ure2p polymerizes to form an amyloid filament backbone surrounded by the C-terminal domains. The latter domains retain their native glutathione-S-transferase (GST)-like fold but are sterically inactivated from their regulatory role in nitrogen catabolism. We have tested this model by differential scanning calorimetry of soluble and filamentous Ure2p and of soluble C-terminal domains, combined with electron microscopy. As predicted, the C-terminal domains respond to thermal perturbation identically in all three states, exhibiting a single endotherm at 76degreesC. In contrast, no thermal signal was associated with the N-terminal domains: in the soluble state of Ure2p, because they are unfolded; in the filamentous state, because their robust amyloid conformation resists heating to 100 degreesC. Published by Elsevier Ltd.