Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.
Laboratory of Agrozoology, Department of Plants and Crops, Ghent University, 9000 Ghent, Belgium.
Int J Mol Sci. 2020 Feb 28;21(5):1659. doi: 10.3390/ijms21051659.
Stress granules are cytoplasmic compartments, which serve as mRNA storage units during stress, therefore regulating translation. The lectin has been widely described as a stress inducible gene. This study aimed to examine in detail the localization of ArathEULS3 lectin in normal and stressed cells. Colocalization experiments revealed that the nucleo-cytoplasmic lectin ArathEULS3 relocates to stress granules after stress. The ArathEULS3 sequence encodes a protein with a EUL lectin domain and an N-terminal domain with unknown structure and function. Bioinformatics analyses showed that the N-terminal domain sequence contains intrinsically disordered regions and likely does not exhibit a stable protein fold. Plasmolysis experiments indicated that ArathEULS3 also localizes to the apoplast, suggesting that this protein might follow an unconventional route for secretion. As part of our efforts we also investigated the interactome of ArathEULS3 and identified several putative interaction partners important for the protein translation process.
应激颗粒是细胞质隔室，在应激期间作为 mRNA 储存单元，从而调节翻译。凝集素已被广泛描述为应激诱导基因。本研究旨在详细检查 AraEULS3 凝集素在正常和应激细胞中的定位。共定位实验表明，核质凝集素 AraEULS3 在应激后重新定位到应激颗粒。AraEULS3 序列编码一种具有 EUL 凝集素结构域和 N 端结构域的蛋白质，该 N 端结构域具有未知的结构和功能。生物信息学分析表明，N 端结构域序列含有内在无序区域，可能不具有稳定的蛋白质折叠。质壁分离实验表明，AraEULS3 还定位于质外体，表明该蛋白可能通过非传统途径进行分泌。作为我们工作的一部分，我们还研究了 AraEULS3 的相互作用组，并鉴定了几个对蛋白质翻译过程重要的假定相互作用伙伴。
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