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酰化作用:一种特定于与质膜相关的猴病毒40大T抗原的新型翻译后修饰。

Acylation: a new post-translational modification specific for plasma membrane-associated simian virus 40 large T-antigen.

作者信息

Klockmann U, Deppert W

出版信息

FEBS Lett. 1983 Jan 24;151(2):257-9. doi: 10.1016/0014-5793(83)80081-7.

Abstract

SV40 transformed mouse cells (mKSA) were labeled in parallel with either [35S]methionine or [3H]palmitate and subfractionated. Nuclear extracts and solubilized plasma membranes were analyzed for the presence of either 35S- or 3H-labeled SV40 large tumor antigen by immunoprecipitation and SDS polyacrylamide gel electrophoresis. The majority of the [35S]methionine labeled large T was recovered from the nuclear fraction, only minor amounts were detected in plasma membranes. In contrast, large T labeled specifically with [3H]palmitate was found only in the plasma membrane fraction. Our results demonstrate a specific acylation of large T associated with plasma membranes, suggesting that the membrane location of this predominantly nuclear protein is specific.

摘要

SV40转化的小鼠细胞(mKSA)用[35S]甲硫氨酸或[3H]棕榈酸酯平行标记并进行亚分级分离。通过免疫沉淀和SDS聚丙烯酰胺凝胶电泳分析核提取物和溶解的质膜中35S或3H标记的SV40大肿瘤抗原的存在情况。大部分[35S]甲硫氨酸标记的大T从核级分中回收,仅在质膜中检测到少量。相反,仅在质膜级分中发现了用[3H]棕榈酸酯特异性标记的大T。我们的结果表明大T与质膜相关的特异性酰化作用,表明这种主要位于细胞核的蛋白质在膜上的定位是特异性的。

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