Centre for Bioinformatics, Pondicherry University, Kalapet, Pondicherry, India.
Department of Biotechnology, Vignan's Foundation for Science, Technology & Research (VFSTR) University, Vadlamudi, Andhra Pradesh, India.
PLoS One. 2018 Mar 14;13(3):e0194335. doi: 10.1371/journal.pone.0194335. eCollection 2018.
Eukaryotic translation initiation factor 2-alpha kinase (EIF2AK) proteins inhibit protein synthesis at translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock, and heat shock. Origin and functional diversification of EIF2AK sequences remain ambiguous. Here we determine the origin and molecular evolution of EIF2AK proteins in lower eukaryotes and studied the molecular basis of divergence among sub-family sequences. Present work emphasized primitive origin of EIF2AK4 sub-family gene in lower eukaryotes of protozoan lineage. Phylogenetic analysis supported common origin and sub-family based classification of EIF2AKs. Functional divergence studies across sub-families revealed several putative amino acid sites, which assist in altered protein interactions of kinase domains. The data can facilitate designing site-directed experimental studies aiming at elucidating diverse functional aspects of kinase domains regarding down-regulation of protein synthesis.
真核翻译起始因子 2-α 激酶 (EIF2AK) 蛋白在翻译起始水平上抑制蛋白质合成，以响应各种应激条件，包括氧化应激、血红素缺乏、渗透压休克和热休克。EIF2AK 序列的起源和功能多样化仍然不清楚。在这里，我们确定了低等真核生物中 EIF2AK 蛋白的起源和分子进化，并研究了亚家族序列之间分歧的分子基础。目前的工作强调了 EIF2AK4 亚家族基因在原生动物谱系中的原始起源。系统发育分析支持 EIF2AK 的共同起源和基于亚家族的分类。跨亚家族的功能分化研究揭示了几个可能的氨基酸位点，这些位点有助于改变激酶结构域的蛋白质相互作用。这些数据可以为设计针对激酶结构域的定向实验研究提供便利，旨在阐明蛋白质合成下调的激酶结构域的不同功能方面。
