Agroécologie, AgroSup Dijon, INRAE, Univ. Bourgogne Franche-Comté, 21000, Dijon, France.
Agroécologie, AgroSup Dijon, CNRS, INRAE, Univ. Bourgogne Franche-Comté, 21000, Dijon, France.
Sci Rep. 2021 Dec 13;11(1):23862. doi: 10.1038/s41598-021-03268-x.
The WEE1 kinase is ubiquitous in plant development and negatively regulates the cell cycle through phosphorylations. However, analogies with the control of the human cell cycle by tyrosine- (Tyr-) phosphorylation of cyclin-dependent kinases (CDKs) are sometimes questioned. In this in silico study, we assessed the structural conservation of the WEE1 protein in the plant kingdom with a particular focus on agronomically valuable plants, the legume crops. We analyzed the phylogenetic distribution of amino-acid sequences among a large number of plants by Bayesian analysis that highlighted the general conservation of WEE1 proteins. A detailed sequence analysis confirmed the catalytic potential of WEE1 proteins in plants. However, some substitutions of an arginine and a glutamate at the entrance of the catalytic pocket, illustrated by 3D structure predictions, challenged the specificity of this protein toward the substrate and Tyr-phosphorylation compared to the human WEE1. The structural differences, which could be responsible for the loss of specificity between human and plants, are highlighted and suggest the involvement of plant WEE1 in more cell regulation processes.
WEE1 激酶在植物发育中普遍存在，并通过磷酸化负调控细胞周期。然而，其对人类细胞周期的酪氨酸（Tyr）磷酸化调控的类似性有时会受到质疑。在这项计算机研究中，我们通过贝叶斯分析评估了植物界 WEE1 蛋白的结构保守性，特别关注具有农业价值的豆类作物。我们通过贝叶斯分析对大量植物的氨基酸序列进行了系统发育分布分析，突出了 WEE1 蛋白的普遍保守性。详细的序列分析证实了 WEE1 蛋白在植物中的催化潜力。然而，通过 3D 结构预测，催化口袋入口处精氨酸和谷氨酸的一些取代，挑战了该蛋白对底物和 Tyr 磷酸化的特异性，与人类 WEE1 相比。结构差异可能导致人类和植物之间特异性的丧失，并表明植物 WEE1 参与了更多的细胞调控过程。
