eEF1Bγs are proteins found in all eukaryotes and have a role in protein translation, being part of the nucleotide exchange factor eEF1B of the elongation factor complex 1. They are unique because of their organization as a fusion between a glutathione transferase (GST) domain and an elongation factor EF1G (PF00647) domain. The main described function of the GST domain in eEF1Bγ is to ensure the proper scaffolding of the different subunits in the eEF1B complex, by interacting with eEF1Bα subunit. Several evidences also suggest that this domain has a role in cellular redox control because it displays enzymatic activity using glutathione as co-substrate. This opens the question of a dual role of eEF1Bγ in cells both in protein translation and stress response, either in a concomitant or competitive way. By analyzing the diversity of eEF1Bγ sequences in fungi, we show that this class of proteins is subjected to diversification within these microorganisms. The challenge is now to understand the impact of such diversification in eEF1Bγ functions both related to protein translation and stress response, and whether this could have driven the ability of fungi to adapt to constraints.

eEF1Bγs 是在所有真核生物中发现的蛋白质，在蛋白质翻译中发挥作用，是延伸因子复合物 1 的核苷酸交换因子 eEF1B 的一部分。延伸因子 EF1G (PF00647) 结构域。eEF1Bγ 中 GST 结构域的主要描述功能是通过与 eEF1Bα 亚基相互作用，确保 eEF1B 复合体中不同亚基的正确支架。一些证据还表明该结构域在细胞氧化还原控制中起作用，因为它使用谷胱甘肽作为共底物显示酶活性。这就提出了 eEF1Bγ 在细胞中以伴随或竞争的方式在蛋白质翻译和应激反应中发挥双重作用的问题。通过分析真菌中 eEF1Bγ 序列的多样性，我们表明这类蛋白质在这些微生物中会发生多样化。现在的挑战是了解这种多样化对与蛋白质翻译和应激反应相关的 eEF1Bγ 功能的影响，以及这是否会驱动真菌适应限制的能力。