THE COAT PROTEIN OF THE YEAST DOUBLE-STRANDED-RNA VIRUS L-A ATTACHES COVALENTLY TO THE CAP STRUCTURE OF EUKARYOTIC MESSENGER-RNA
THE COAT PROTEIN OF THE YEAST DOUBLE-STRANDED-RNA VIRUS L-A ATTACHES COVALENTLY TO THE CAP STRUCTURE OF EUKARYOTIC MESSENGER-RNA
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DOI：
10.1128/mcb.12.8.3390
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发表时间：
1992-08-01
影响因子：
5.3
通讯作者：
SONENBERG, N
中科院分区：
文献类型：
--
作者：
BLANC, A;GOYER, C;SONENBERG, N
真核生物mRNA 5'帽结构m7 GpppX（其中X是任何核苷酸）与许多细胞蛋白相互作用。 在哺乳动物、酵母和果蝇细胞中研究了其中几种蛋白质，发现它们参与翻译起始。 在这里，我们描述了一种新的帽结合蛋白，外壳蛋白的L-A，一种双链RNA病毒，是持久地保持在许多酿酒酵母菌株。 结果还表明，相关的双链RNA病毒（L-BC）的外壳蛋白同样是帽结合蛋白。 引人注目的是，与细胞帽结合蛋白相反，L-A病毒外壳蛋白和帽结构之间的相互作用是通过共价键。
The eukaryotic mRNA 5' cap structure m7GpppX (where X is any nucleotide) interacts with a number of cellular proteins. Several of these proteins were studied in mammalian, yeast, and drosophila cells and found to be involved in translation initiation. Here we describe a novel cap-binding protein, the coat protein of L-A, a double-stranded RNA virus that is persistently maintained in many Saccharomyces cerevisiae strains. The results also suggest that the coat protein of a related double-stranded RNA virus (L-BC) is likewise a cap-binding protein. Strikingly, in contrast to the cellular cap-binding proteins, the interaction between the L-A virus coat protein and the cap structure is through a covalent bond.