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翻译起始因子eIF_5A在真核细胞内普遍存在 ,是目前为止惟一发现含独特氨基酸hypusine残基的蛋白。hypusine是eIF_5A前体的特定赖氨酸残基 (第 5 0位 )经亚精胺依赖性的翻译后修饰形成的 ,每一成熟的eIF_5A仅含一个hypusine残基 ,eIF_5A的hypusine修饰是其发挥功能、细胞存活和增殖所必需的。本文对eIF_5A的研究历史、现状和hypusine功能的近期进展进行了概述 ,并进一步分析了eIF_5A的可能功能及hypusine修饰过程作为药物靶标诱导细胞凋亡的应用前景。
The translation initiation factor eIF_5A is ubiquitous in eukaryotic cells and is by far the only protein found to contain a hypusine residue with a unique amino acid. Hypusine is a spermine-dependent post-translational modification of a specific lysine residue (at position 50) of the eIF-5A precursor, with only one hypusine residue per mature eIF-5A and hypusine modification of eIF-5A Function, cell survival and proliferation necessary. This review summarizes the recent history of eIF_5A research and its current status and hypusine function, and further analyzes the possible function of eIF_5A and hypofluorine modification process as drug targets to induce apoptosis.