Hannig E M
Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson 75083-0688, USA.
Bioessays. 1995 Nov;17(11):915-9. doi: 10.1002/bies.950171103.
The pathway for initiation of protein synthesis in eukaryotic cells has been defined and refined over the last 25 years using purified components and in vitro reconstituted systems. More recently, powerful genetic analysis in yeast has proved useful in unraveling aspects of translation inherently more difficult to address by strictly biochemical approaches. One area in particular is the functional analysis of multi-subunit protein factors, termed eukaryotic initiation factors (eIFs), that play an essential role in translation initiation. eIF-3, the most structurally complex of the eIFs, has until recently eluded this approach. The identification of the yeast GCD10 gene as the structural gene for the zeta subunit of yeast eIF-3(1) and the analysis of mutant phenotypes has opened the door to the genetic dissection of the eIF-3 protein complex.
在过去25年里，利用纯化的组分和体外重构系统，真核细胞中蛋白质合成起始途径已得到明确和完善。最近，酵母中强大的遗传分析已证明，对于解析翻译过程中一些本质上难以通过严格生化方法解决的方面很有用。特别值得一提的是多亚基蛋白质因子（称为真核起始因子，即eIFs）的功能分析，这些因子在翻译起始中起关键作用。eIF-3是eIFs中结构最复杂的一个，直到最近这种方法都难以对其进行研究。酵母GCD10基因被鉴定为酵母eIF-3ζ亚基的结构基因，对突变体表型的分析为eIF-3蛋白复合体的遗传剖析打开了大门。
