Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro.
Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro.
复制标题
脱水蛋白、CdDHN4-L 和 CdDHN4-S 的表征及其体外对抗非生物胁迫的不同保护作用
DOI：
10.1186/s12870-018-1511-2
复制
发表时间：
2018-11-26
影响因子：
5.3
通讯作者：
Zhou P
中科院分区：
文献类型：
--
作者：
Lv A;Su L;Liu X;Xing Q;Huang B;An Y;Zhou P
脱水剂在调节植物的非生物胁迫反应中起着积极的作用。本研究的目的是表征两个脱氢基因，CdDHN4- l和CdDHN4- s，由CdDHN4选择性剪接在百慕大草中产生。过表达φ-片段的CdDHN4-L和φ-片段缺失的CdDHN4-S可显著提高拟南芥对非生物胁迫的耐受性。100 mM NaCl处理下，过表达CdDHN4-L的拟南芥的生长表型优于过表达CdDHN4-S的拟南芥，在300和400 mM NaCl处理下，过表达CdDHN4-L的大肠杆菌细胞的生长表型优于过表达CdDHN4-S的细胞，并在- 20℃和50℃的极端温度条件下进行处理。在10 ~ 90℃范围内，CdDHN4-L的结构无序性高于CdDHN4-S。CdDHN4-L和CdDHN4-S对乳酸脱氢酶（LDH）和醇脱氢酶（ADH）在冻融损伤和加热条件下的恢复活性均高于LDH和ADH。蛋白结合和双分子荧光互补表明，两种蛋白均可通过静电力与带正等电点的蛋白结合。这些结果表明，与CdDHN4-S相比，CdDHN4-L具有更高的柔性展开结构和热稳定性，对非生物胁迫具有更高的保护能力。这些结果直接证明了脱水剂中φ-片段在保护植物免受非生物胁迫方面的作用，并揭示了脱水剂与客户蛋白之间的静电相互作用。本文的在线版本（10.1186/s12870-018-1511-2）包含补充内容，授权用户可使用。
Dehydrins play positive roles in regulating plant abiotic stress responses. The objective of this study was to characterize two dehydrin genes, CdDHN4-L and CdDHN4-S, generated by alternative splicing of CdDHN4 in bermudagrass. Overexpression of CdDHN4-L with φ-segment and CdDHN4-S lacking of φ-segment in Arabidopsis significantly increased tolerance against abiotic stresses. The growth phenotype of Arabidopsis exposed to NaCl at 100 mM was better in plants overexpressing CdDHN4-L than those overexpressing CdDHN4-S, as well as better in E.coli cells overexpressing CdDHN4-L than those overexpressing CdDHN4-S in 300 and 400 mM NaCl, and under extreme temperature conditions at − 20 °C and 50 °C. The CdDHN4-L had higher disordered characterization on structures than CdDHN4-S at temperatures from 10 to 90 °C. The recovery activities of lactic dehydrogenase (LDH) and alcohol dehydrogenase (ADH) in presence of CdDHN4-L and CdDHN4-S were higher than that of LDH and ADH alone under freeze-thaw damage and heat. Protein-binding and bimolecular fluorescence complementation showed that both proteins could bind to proteins with positive isoelectric point via electrostatic forces. These results indicate that CdDHN4-L has higher protective ability against abiotic stresses due to its higher flexible unfolded structure and thermostability in comparison with CdDHN4-S. These provided direct evidence of the function of the φ-segment in dehydrins for protecting plants against abiotic stress and to show the electrostatic interaction between dehydrins and client proteins. The online version of this article (10.1186/s12870-018-1511-2) contains supplementary material, which is available to authorized users.
登录
查看更多内容
影响因子：
4.9
作者：
Liu, Guobao;Xu, Hong;Zheng, Yizhi
通讯作者：
Zheng, Yizhi
影响因子：
5.6
作者：
Hernández-Sánchez IE;Maruri-López I;Ferrando A;Carbonell J;Graether SP;Jiménez-Bremont JF
通讯作者：
Jiménez-Bremont JF
影响因子：
4.6
作者：
Liu Y;Wang L;Zhang T;Yang X;Li D
通讯作者：
Li D
影响因子：
7.2
作者：
Clough, SJ;Bent, AF
通讯作者：
Bent, AF
CdDHN4（一种来自狗牙根的新型 YSK2 型脱水蛋白基因）的表达，通过 ABA 依赖性信号途径响应干旱胁迫
影响因子：
5.6
作者：
Lv A;Fan N;Xie J;Yuan S;An Y;Zhou P
通讯作者：
Zhou P