Eukaryotic elongation factor 1A (eEF1A) is an essential and highly conserved protein involved in diverse cellular processes, including translation, cytoskeleton organisation, nuclear export, and proteasomal degradation. Recently, nine novel and site-specific methyltransferases were discovered that target eEF1A, five in yeast and four in human, making it the eukaryotic protein with the highest number of independent methyltransferases. Some of these methyltransferases show striking evolutionary conservation. Yet, they come from diverse methyltransferase families, indicating they confer competitive advantage through independent origins. As might be expected, the first functional studies of specific methylation sites found them to have distinct effects, notably on eEF1A-related processes of translation and tRNA aminoacylation. Further functional studies of sites will likely reveal other unique roles for this interesting modification.

真核生物延伸因子1A（eEF1A）是一种重要且高度保守的蛋白质，涉及多种细胞过程，包括翻译，细胞骨架组织，核输出和蛋白酶体降解。最近，发现了九种新的和特定于位点的甲基转移酶，它们靶向eEF1A，其中五个在酵母中，四个在人类中，使其成为具有最多独立甲基转移酶数量的真核蛋白。这些甲基转移酶中的一些显示出惊人的进化保守性。然而，它们来自不同的甲基转移酶家族，表明它们通过独立的起源赋予了竞争优势。可以预期，对特定甲基化位点的首次功能研究发现它们具有独特的作用，特别是对eEF1A相关的翻译和tRNA氨基酰化过程。