仙台病毒粒子转录酶复合体：多肽组成及病毒粒子包膜蛋白的抑制作用
Sendai virion transcriptase complex: polyeptide composition and inhibition by virion envelope proteins.
作者信息
Marx P A, Portner A, Kingsbury D W
出版信息
J Virol. 1974 Jan;13(1):107-12. doi: 10.1128/JVI.13.1.107-112.1974.
Abstract
Sendai virions, disrupted in 2% Triton X-100 in 1 M KCl, were separated into nucleocapsids and envelope proteins by centrifugation. The nucleocapsids, representing 46% of the virion proteins, had a buoyant density of 1.29 gm/cm(3) in D(2)O sucrose. RNA-dependent transcriptase activity associated with them had a ninefold greater specific activity than transcriptase assayed in unfractionated detergent-disrupted virions. These enzyme-active nucleocapsids contained only two polypeptides, the largest virion polypeptide (molecular weight 75,000) and the nucleocapsid structure unit (molecular weight 60,000). Virion envelope proteins, either glycoproteins or nonglycosylated matrix protein, inhibited nucleocapsid-associated polymerase activity; brief heat denaturation abolished their inhibitory activity. Yeast RNA stimulated nucleocapsid-associated enzyme, suggesting that stimulatory polyanions act at the enzyme-template level.
摘要
将仙台病毒粒子在含有1M氯化钾的2% Triton X-100中裂解，通过离心将其分离为核衣壳和包膜蛋白。核衣壳占病毒粒子蛋白的46%，在重水蔗糖中的浮力密度为1.29克/立方厘米。与它们相关的RNA依赖性转录酶活性比在未分级的去污剂裂解病毒粒子中测定的转录酶比活性高九倍。这些具有酶活性的核衣壳仅包含两种多肽，即最大的病毒粒子多肽（分子量75,000）和核衣壳结构单元（分子量60,000）。病毒粒子包膜蛋白，无论是糖蛋白还是非糖基化基质蛋白，都抑制核衣壳相关的聚合酶活性；短暂的热变性消除了它们的抑制活性。酵母RNA刺激核衣壳相关酶，表明刺激性聚阴离子在酶-模板水平起作用。
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