State Key Laboratory of Agrobiotechnology and School of Life Sciences, The Chinese University of Hong Kong, Shatin, Hong Kong.
Plant Biol (Stuttg). 2013 Jan;15(1):13-8. doi: 10.1111/j.1438-8677.2012.00606.x. Epub 2012 Jun 5.
Phosphorylation of eIF2α is an important strategy for living organisms to adapt to metabolic and physiological changes that are often associated with external stimuli. GCN2 is one of the well-studied eIF2α kinases in yeast and mammals, which is responsible for the survival of the organism under amino acid starvation. Despite the downstream reactions being quite divergent, AtGCN2 exhibits a high primary sequence similarity to its yeast and animal counterparts. In this study, we provide experimental evidence to show that AtGCN2 shares similar biochemical properties to the yeast and animal homologues. Our in vitro assays demonstrate the binding of the C-terminus of AtGCN2 to uncharged tRNA molecules and the enzymatic activities of AtGCN2 on both eIF2α homologues in A. thaliana, thus providing essential information for further understanding the functions of plant general control non-repressible (GCN) homologues.
真核起始因子 2α 的磷酸化是生物适应代谢和生理变化的重要策略，这些变化通常与外部刺激有关。GCN2 是酵母和哺乳动物中研究较为深入的 eIF2α 激酶之一，它负责在氨基酸饥饿时维持生物体的生存。尽管下游反应差异很大，但 AtGCN2 与酵母和动物同源物具有高度的一级序列相似性。在这项研究中，我们提供了实验证据表明 AtGCN2 具有与酵母和动物同源物相似的生化特性。我们的体外测定表明 AtGCN2 的 C 末端与不带电荷的 tRNA 分子结合，并且 AtGCN2 在拟南芥中的两种 eIF2α 同源物上具有酶活性，从而为进一步了解植物一般控制非抑制性（GCN）同源物的功能提供了重要信息。
