Cloning and Characterization of a gene Encoding True D-cysteine Desulfhydrase from Oryza sativa

文献类型： 外文期刊

第一作者： Zhou, Heng

作者： Zhou, Heng;Guan, Wenxue;Wu, Deliang;Yin, Xianchao;Zhou, Heng;Guan, Wenxue;Zhou, Mingjian;Shen, Jie;Wu, Deliang;Xie, Yanjie;Liu, Xin

作者机构：

关键词： D-cysteine desulfhydrase; Hydrogen sulfide; 1-aminocyclopropane-1-carboxylate deaminase; Subcellular localization

期刊名称：PLANT MOLECULAR BIOLOGY REPORTER （ 影响因子：1.595； 五年影响因子：2.042 ）

ISSN： 0735-9640

年卷期： 2020 年 38 卷 1 期

页码：

收录情况： SCI

摘要： Hydrogen sulfide (H2S) has been regarded as the third gasotransmitter and plays an active role in multiple signaling events of plants and animals. Cysteine desulfhydrases (CDes), including both D- and L-cysteine desulfhydrases (D/L-CDes) that degrade L- or D-cysteine into H2S, pyruvate, and ammonium, are considered the key enzymes responsible for endogenous H2S generation in plants. Several D-CDes are homologous to 1-aminocyclopropane-1-carboxylate deaminase (ACCD) and possess both ACCD and D-CDes activities, thus not a real specific D-CDes. However, little attention had been paid to true D-CDes and little information has been known about this protein in plants. In this study, a putative D-CDes transcript was cloned and characterized from Oryza sativa which encodes a protein with 423 amino acids possessing D-CDes activity and named as OsDCD1. Neither activities of ACCD nor O-acetyl-L-serine (thiol) lyase (OASTL) can be detected from OsDCD1 recombinant protein. For D-Cys, the K-m of OsDCD1 is 0.13 +/- 0.01 mM and the V-m is 111.55 +/- 1.91 units mg(-1) of protein. The pH-optimum and temperature-optimum of the OsDCD1 are 8.5 and 35 degrees C, respectively. By site-directed mutagenesis, mutation of S357E or S357E/T589L almost fully abolished the D-CDes activity of OsDCD1, while the T389L mutant retained only partial D-CDes activity by 3.7%, indicating these two amino acid residues play critical roles for the maintenance of OsDCD1 activity. Besides, subcellular localization analysis in rice protoplast revealed that the OsDCD1 localizes in the chloroplast but not mitochondria, which is different from DCD1 in Arabidopsis. The qRT-PCR analysis further showed that the abundance of OsDCD1 transcript was widely regulated by different hormones and chemical reagents we used. In general, our results provided evidence that OsDCD1 is a potentially important endogenous H2S producing enzyme in rice, which may play an important role in plant growth regulators and chemical stimuli.

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