Multistep nucleus formation and a separate subunit contribution of the amyloidgenesis of heat-denatured monellin
Multistep nucleus formation and a separate subunit contribution of the amyloidgenesis of heat-denatured monellin
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DOI：
10.1110/ps.20201
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发表时间：
2001-10-01
期刊：
影响因子：
8
通讯作者：
Konno, T
中科院分区：
文献类型：
--
作者：
Konno, T
Monellin(MN)是一种甜味的植物蛋白，已知在热变性状态下形成纤维聚集体。在这里，广泛地描述了MN的淀粉型聚集过程。淀粉样蛋白的形成是在MN高度变性的状态下开始的。跳过淀粉样蛋白形成动力学的标记阶段的种子效应建立了依赖于成核的聚集机制。一项严格控制的实验方案显示，在核成熟之前还有一个额外的前核阶段，表明最初的滞后阶段由多个构象事件组成。对MN和重组单链MN单独的A和B亚单位链的聚集性质的研究结果表明，B链是淀粉样蛋白类型聚集的唯一贡献者。这些发现为MN及其亚基的Arnyloid发生提供了一种方案，并提供了一种独特的受蛋白质亚单位组成调控的Arnyloid发生模式。
Monellin (MN) is a sweet-tasting plant protein known to form fibrous aggregates in the heat-denatured state. Here the amyloid-type aggregation process of MN is extensively characterized. The amyloidgenesis was initiated in a highly denatured state of MN. A seeding effect of Skipping a tag phase of the amyloid formation kinetics established a nucleation-dependent aggregation mechanism. A finely controlled experimental protocol revealed an additional prenucleus stage preceding the maturation of the nucleus, indicating that the initial lag phase is composed of multiple conformational events. The results obtained for the aggregation properties of the separate A and B subunit chains of MN and a recombinant single-chain MN suggest that the B chain exclusively contributed to the amyloid-type aggregation. These findings suggest a scheme for the arnyloidgenesis of MN and their subunits, and provide a unique model of arnyloidgenesis that is regulated by the subunit composition of protein.