Nonstructural proteins of Semliki Forest virus: synthesis, processing, and stability in infected cells
Nonstructural proteins of Semliki Forest virus: synthesis, processing, and stability in infected cells
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塞姆利基森林病毒的非结构蛋白：受感染细胞中的合成、加工和稳定性
DOI：
10.1128/jvi.47.3.505-515.1983
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发表时间：
1983
影响因子：
5.4
通讯作者：
Laura Ruohonen
中科院分区：
文献类型：
--
作者：
Sirkka KERANENt;Laura Ruohonen
本文研究了塞姆利基森林病毒（Semliki Forest virus）非结构蛋白（NS）的体内合成。第四个ns蛋白，ns 60，被鉴定和分离。翻译顺序（NH 2-ns 70-ns 86-ns 60-ns 72-COOH）通过在翻译起始的高渗阻断之后或存在下使用各种标记程序来确定。设计了一种顺序标记程序，以特异性地标记多蛋白的限定片段。特定的标记程序允许分离的四个NS蛋白的放射化学纯的形式，在十二烷基硫酸钠的存在下，通过梯度聚丙烯酰胺凝胶电泳。经金黄色葡萄球菌V8蛋白酶消化后，四种ns蛋白具有不同的一级结构。通过脉冲追踪实验研究了ns多聚蛋白的加工过程和ns成熟蛋白的稳定性。在多肽链翻译后2至3分钟内，每种蛋白质从多蛋白中裂解。N-末端蛋白ns 70以其成熟形式出现，晚于ns 86，ns 86在多聚蛋白中紧随其后，这表明ns 70经历了翻译后修饰。的C-末端蛋白，ns 72，立即脉冲后的迁移略快于追逐后，这表明ns 72也经历了翻译后修饰以外的切割。ns 72的半衰期比其他ns蛋白短。
The synthesis of the nonstructural (ns) proteins of Semliki Forest virus was studied in vivo. The fourth ns protein, ns60, was identified and isolated. The order of translation (NH2-ns70-ns86-ns60-ns72-COOH) was determined by using various labeling procedures after or in the presence of a hypertonic block of translation initiation. A sequential labeling procedure was devised to specifically label defined segments of the polyprotein. The specific labeling procedures allowed isolation of the four ns proteins in radiochemically pure form by gradient polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The four ns proteins were shown to have different primary structures by digestion with V8 protease of Staphylococcus aureus. The processing of the ns polyprotein and the stability of the mature ns proteins were studied by pulse-chase experiments. The cleavage of each of the proteins from the polyprotein took place within 2 to 3 min after the translation of the polypeptide chain. The N-terminal protein, ns70, appeared in its mature form later than ns86, which follows it in the polyprotein, suggesting that ns70 undergoes a post-translational modification. The migration of the C-terminal protein, ns72, immediately after a pulse was slightly faster than after a chase, suggesting that ns72 also undergoes a post-translational modification other than a cleavage. The half-life of ns72 was shorter than that of the other ns proteins.
影响因子：
3.7
作者：
Fuller,FJ;Marcus,PI
通讯作者：
Marcus,PI