真核生物翻译起始：每个故事（至少）都有两面性。

Eukaryotic translation initiation: there are (at least) two sides to every story.

作者信息

Sachs A B, Varani G

机构信息

Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.

出版信息

Nat Struct Biol. 2000 May;7(5):356-61. doi: 10.1038/75120.

DOI:10.1038/75120

PMID:10802729

Abstract

The eukaryotic cap and poly(A) tail binding proteins, eIF4E and Pab1p, play important roles in the initiation of protein synthesis. The recent structures of the complex of eIF4E bound to the methylated guanosine (cap) found at the 5'end of messenger RNA (mRNA), the complex of eIF4E bound to peptide fragments of two related translation factors (eIF4G and 4E-BP1), and the complex of the N-terminal fragment of Pab1p bound to polyadenylate RNA have revealed that eIF4E and Pab1p contain at least two distinct functional surfaces. One surface is used for binding mRNA, and the other for binding proteins involved in translation initiation.

摘要

真核生物的帽结合蛋白和聚腺苷酸尾结合蛋白，即eIF4E和Pab1p，在蛋白质合成起始过程中发挥重要作用。最近，与信使核糖核酸（mRNA）5'端甲基化鸟苷（帽）结合的eIF4E复合物、与两个相关翻译因子（eIF4G和4E-BP1）的肽片段结合的eIF4E复合物，以及与聚腺苷酸RNA结合的Pab1p N端片段复合物的结构表明，eIF4E和Pab1p至少包含两个不同的功能表面。一个表面用于结合mRNA，另一个用于结合参与翻译起始的蛋白质。