Blanc A, Goyer C, Sonenberg N
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Mol Cell Biol. 1992 Aug;12(8):3390-8. doi: 10.1128/mcb.12.8.3390-3398.1992.
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.
真核生物信使核糖核酸(mRNA)的5'帽结构m7GpppX(其中X为任意核苷酸)与多种细胞蛋白相互作用。在哺乳动物、酵母和果蝇细胞中对其中几种蛋白进行了研究,发现它们参与翻译起始过程。在此,我们描述一种新型帽结合蛋白,即L-A双链RNA病毒的外壳蛋白,该病毒在许多酿酒酵母菌株中持续存在。结果还表明,相关双链RNA病毒(L-BC)的外壳蛋白同样是一种帽结合蛋白。引人注目的是,与细胞帽结合蛋白不同,L-A病毒外壳蛋白与帽结构之间的相互作用是通过共价键实现的。