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真核生物起始因子eIF-2和eIF-3:核糖体起始复合物中的相互作用、结构与定位

Eukaryotic initiation factors eIF-2 and eIF-3: interactions, structure and localization in ribosomal initiation complexes.

作者信息

Bommer U A, Lutsch G, Stahl J, Bielka H

机构信息

Institute of Molecular Biology, Berlin-Buch, Germany.

出版信息

Biochimie. 1991 Jul-Aug;73(7-8):1007-19. doi: 10.1016/0300-9084(91)90142-n.

Abstract

More than ten different protein factors are involved in initiation of protein synthesis in eukaryotes. For binding of initiator tRNA and mRNA to the 40S ribosomal subunit, the initiation factors eIF-2 and eIF-3 are particularly important. They consist of several different subunits and form stable complexes with the 40S ribosomal subunit. The location of eIF-2 and eIF-3 in these complexes as well as the interactions of the individual components have been analyzed by biochemical methods and electron microscopy. The results obtained are summarized in this article, and a model is derived describing the spatial arrangement of eIF-2 and eIF-3 together with initiator tRNA and mRNA on the 40S subunit. Conclusions on the location of functionally important sites of eukaryotic small ribosomal subunits are discussed with regard to the respective location of these sites in the prokaryotic counterpart.

摘要

十多种不同的蛋白质因子参与真核生物蛋白质合成的起始过程。对于起始tRNA和mRNA与40S核糖体亚基的结合,起始因子eIF-2和eIF-3尤为重要。它们由几个不同的亚基组成,并与40S核糖体亚基形成稳定的复合物。通过生化方法和电子显微镜分析了eIF-2和eIF-3在这些复合物中的位置以及各个组分之间的相互作用。本文总结了所获得的结果,并推导了一个模型,描述了eIF-2和eIF-3与起始tRNA和mRNA在40S亚基上的空间排列。关于真核小核糖体亚基功能重要位点的位置,本文结合这些位点在原核对应物中的各自位置进行了讨论。

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