不同因子與核糖體相關(guān)聯(lián)，來幫助蛋白鏈的啟動(dòng),、延伸和終止,。教科書上對(duì)蛋白合成的解釋只描述了兩個(gè)普遍保守的“翻譯延伸因子”，即EF-Tu/eEF1A 和 EF-G/eEF2,。
現(xiàn)在,，對(duì)釀酒酵母的蛋白合成所做的一項(xiàng)研究,，重新將一個(gè)以前被認(rèn)為與啟動(dòng)過程相關(guān)的因子（eIF5A）定位為延伸過程中的一個(gè)核心因子。eIF5A的不尋常之處是,，它含有一個(gè)罕見的氨基酸,，即Hypusine，eIF5A必須有這種氨基酸才能夠刺激延伸,。根據(jù)在缺少eIF5A時(shí)所觀察到的缺陷,，研究人員提出，這個(gè)因子可能與eEF2一起在轉(zhuǎn)位過程中發(fā)揮功能,。（生物谷Bioon.com）
生物谷推薦原始出處：
Nature 459, 118-121 (7 May 2009) | doi:10.1038/nature08034
Hypusine-containing protein eIF5A promotes translation elongation
Preeti Saini1, Daniel E. Eyler2, Rachel Green2 & Thomas E. Dever1
1 Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA
2 Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Translation elongation factors facilitate protein synthesis by the ribosome. Previous studies identified two universally conserved translation elongation factors, EF-Tu in bacteria (known as eEF1A in eukaryotes) and EF-G (eEF2), which deliver aminoacyl-tRNAs to the ribosome and promote ribosomal translocation, respectively1. The factor eIF5A (encoded by HYP2 and ANB1 in Saccharomyces cerevisiae), the sole protein in eukaryotes and archaea to contain the unusual amino acid hypusine (N -(4-amino-2-hydroxybutyl)lysine)2, was originally identified based on its ability to stimulate the yield (endpoint) of methionyl-puromycin synthesis—a model assay for first peptide bond synthesis thought to report on certain aspects of translation initiation3, 4. Hypusine is required for eIF5A to associate with ribosomes5, 6 and to stimulate methionyl-puromycin synthesis7. Because eIF5A did not stimulate earlier steps of translation initiation8, and depletion of eIF5A in yeast only modestly impaired protein synthesis9, it was proposed that eIF5A function was limited to stimulating synthesis of the first peptide bond or that eIF5A functioned on only a subset of cellular messenger RNAs. However, the precise cellular role of eIF5A is unknown, and the protein has also been linked to mRNA decay, including the nonsense-mediated mRNA decay pathway10, 11, and to nucleocytoplasmic transport12, 13. Here we use molecular genetic and biochemical studies to show that eIF5A promotes translation elongation. Depletion or inactivation of eIF5A in the yeast S. cerevisiae resulted in the accumulation of polysomes and an increase in ribosomal transit times. Addition of recombinant eIF5A from yeast, but not a derivative lacking hypusine, enhanced the rate of tripeptide synthesis in vitro. Moreover, inactivation of eIF5A mimicked the effects of the eEF2 inhibitor sordarin, indicating that eIF5A might function together with eEF2 to promote ribosomal translocation. Because eIF5A is a structural homologue of the bacterial protein EF-P14, 15, we propose that eIF5A/EF-P is a universally conserved translation elongation factor.
