S-nitrosation Impairs Activity of Stress-inducible Aldehyde Dehydrogenases from Arabidopsis thaliana,Plant Science

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S-nitrosation Impairs Activity of Stress-inducible Aldehyde Dehydrogenases from Arabidopsis thaliana
Plant Science ( IF 4.2 ) Pub Date : 2020-03-01 , DOI: 10.1016/j.plantsci.2019.110389
Naïm Stiti ₁ , Karolina Anna Podgórska ₁ , Dorothea Bartels ₁

Affiliation

Nitric oxide (NO) is an intracellular messenger that mediates stress responses. Several plant aldehyde dehydrogenase (ALDH) genes are expressed during abiotic stress conditions to reduce the level of cytotoxic aldehydes. We investigated a possible interference between NO and ALDHs, using the isoform ALDH3H1 of Arabidopsis thaliana as model. The physiological NO donor; S-nitrosoglutathione (GSNO), inhibits ALDH3H1 in a time- and concentration-dependent manner. Mutagenesis and ESI-MS/MS analyses show that all Cys residues of ALDH3H1 are targets of GSNO-mediated S-nitrosation. Chemical labelling indicates that the deactivation is due to the conversion of the catalytic thiol into a catalytically non-active nitrosothiol. GSNO has the same effect on the chloroplastic ALDH3I1, suggesting that susceptibility of the catalytic Cys to NO is a common feature of ALDHs. S-Nitrosation and enzymatic inhibition of ALDH were reverted by reducing agents. Our study proves that the function of ALDHs does not exclusively depend on transcriptional regulation, with stress-induced expression, but may be also susceptible to posttranslational regulation through S-nitrosation. We discuss the potential involvement of S-nitrosoglutathione reductase (GSNOR), binding specific cofactors and reducing partners in a protective system of ALDHs in vivo, which will be experimentally corroborated in our forthcoming study.

中文翻译：

S-亚硝化损害拟南芥胁迫诱导型醛脱氢酶的活性

一氧化氮 (NO) 是一种介导应激反应的细胞内信使。几种植物醛脱氢酶 (ALDH) 基因在非生物胁迫条件下表达，以降低细胞毒性醛的水平。我们使用拟南芥的同种型 ALDH3H1 作为模型，研究了 NO 和 ALDH 之间可能的干扰。生理 NO 供体；S-亚硝基谷胱甘肽 (GSNO) 以时间和浓度依赖性方式抑制 ALDH3H1。诱变和 ESI-MS/MS 分析表明 ALDH3H1 的所有 Cys 残基都是 GSNO 介导的 S-亚硝化的目标。化学标记表明失活是由于催化硫醇转化为无催化活性的亚硝基硫醇。GSNO 对叶绿体 ALDH3I1 具有相同的作用，这表明催化性 Cys 对 NO 的敏感性是 ALDHs 的一个共同特征。ALDH 的 S-亚硝化作用和酶促抑制作用被还原剂逆转。我们的研究证明，ALDHs 的功能不仅仅依赖于转录调控，应激诱导的表达，而且可能也容易受到 S-亚硝化的翻译后调控。我们讨论了 S-亚硝基谷胱甘肽还原酶 (GSNOR)、结合特定辅因子和还原伙伴在体内 ALDH 保护系统中的潜在参与，这将在我们即将进行的研究中得到实验证实。但也可能容易受到 S-亚硝化作用的翻译后调控。我们讨论了 S-亚硝基谷胱甘肽还原酶 (GSNOR)、结合特定辅因子和还原伙伴在体内 ALDH 保护系统中的潜在参与，这将在我们即将进行的研究中得到实验证实。但也可能容易受到 S-亚硝化作用的翻译后调控。我们讨论了 S-亚硝基谷胱甘肽还原酶 (GSNOR)、结合特定辅因子和还原伙伴在体内 ALDH 保护系统中的潜在参与，这将在我们即将进行的研究中得到实验证实。

更新日期：2020-03-01

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