Translation elongation factor P (EF-P) is conserved in all three domains of life (called eIF5A and aIF5A in eukaryotes and archaea, respectively) and functions to alleviate ribosome pausing during the translation of specific sequences, including consecutive proline residues. EF-P was identified in 1975 as a factor that stimulated the peptidyltransferase reaction in vitro but its involvement in the translation of tandem proline residues was not uncovered until 2013. Throughout the four decades of EF-P research, perceptions of EF-P function have changed dramatically. In particular, while EF-P was thought to potentiate the formation of the first peptide bond in a protein, it is now broadly accepted to act throughout translation elongation. Further, EF-P was initially reported to be essential, but recent work has shown that the requirement of EF-P for growth is conditional. Finally, it is thought that post-translational modification of EF-P is strictly required for its function but recent studies suggest that EF-P modification may play a more nuanced role in EF-P activity. Here, we review the history of EF-P research, with an emphasis on its initial isolation and characterization as well as the discoveries that altered our perceptions of its function.

中文翻译：

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翻译延伸因子P（EF-P）。

翻译延伸因子P（EF-P）在生命的所有三个域中均处于保守状态（在真核生物和古细菌中分别称为eIF5A和aIF5A），并具有缓解特定序列翻译过程中核糖体停顿的功能，包括连续的脯氨酸残基。EF-P于1975年被确定为刺激体外肽基转移酶反应的因子但是直到2013年才发现它参与了串联脯氨酸残基的翻译。在EF-P研究的四十年中，人们对EF-P功能的认识发生了巨大变化。尤其是，尽管人们认为EF-P可以增强蛋白质中第一个肽键的形成，但现在人们普遍认为它可以在整个翻译过程中发挥作用。此外，最初报道了EF-P是必不可少的，但是最近的研究表明EF-P对生长的需求是有条件的。最后，人们认为EF-P的翻译后修饰是其功能的严格要求，但最近的研究表明EF-P修饰可能在EF-P活性中起更细微的作用。在这里，我们回顾了EF-P研究的历史，