Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms

文献类型： 外文期刊

第一作者： Liu, Yingying

作者： Liu, Yingying;Zhang, Heng;Han, Jiahui;Jiang, Shijie;Geng, Xiuxiu;Xue, Dong;Chen, Yun;Zhang, Chen;Zhou, Zhengfu;Zhang, Wei;Chen, Ming;Lin, Min;Wang, Jin;Jiang, Shijie;Geng, Xiuxiu

作者机构：

期刊名称：MICROBIAL BIOTECHNOLOGY （ 影响因子：5.813； 五年影响因子：6.559 ）

ISSN： 1751-7915

年卷期： 2019 年 12 卷 4 期

页码：

收录情况： SCI

摘要： Late embryogenesis abundant (LEA) proteins play a protective role during desiccation and oxidation stresses. LEA3 proteins are a major group characterized by a hydrophilic domain (HD) with a highly conserved repeating 11-amino acid motif. We compared four different HD orthologs from distant organisms: (i) DrHD from the extremophilic bacterium Deinococcus radiodurans; (ii) CeHD from the nematode Caenorhabditis elegans; (iii) YlHD from the yeast Yarrowia lipolytica; and (iv) BnHD from the plant Brassica napus. Circular dichroism spectroscopy showed that all four HDs were intrinsically disordered in phosphate buffer and then folded into alpha-helical structures with the addition of glycerol or trifluoroethanol. Heterologous HD expression conferred enhanced desiccation and oxidation tolerance to Escherichia coli. These four HDs protected the enzymatic activities of lactate dehydrogenase (LDH) by preventing its aggregation under desiccation stress. The HDs also interacted with LDH, which was intensified by the addition of hydrogen peroxide (H2O2), suggesting a protective role in a chaperone-like manner. Based on these results, the HDs of LEA3 proteins show promise as protectants for desiccation and oxidation stresses, especially DrHD, which is a potential ideal stress-response element that can be applied in synthetic biology due to its extraordinary protection and stress resistance ability.

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