Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice

doi:10.1016/S1671-2927(00)8675

Journal of Integrative Agriculture ›› 2012, Vol. 12 ›› Issue (9): 1434-1444.DOI: 10.1016/S1671-2927(00)8675

Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice

YANG Sheng-hui, NIU Xiang-li, LUO Di, CHEN Chang-dong, YU Xu, TANG Wei, LU Bao-rong, LIU Yong-sheng

1.Key Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R.China
2.College of Life Sciences, Chongqing University, Chongqing 400044, P.R.China
3.Key Laboratory for Biodiversity Science and Ecological Engineering, Ministry of Education/Institute of Biodiversity Science, Fudan University, Shanghai 200433, P.R.China

收稿日期:2011-04-28 出版日期:2012-09-01 发布日期:2012-09-09
通讯作者: Correspondence LIU Yong-sheng, Tel/Fax: +86-28-85460570, E-mail:liuyongsheng1122@yahoo.com.cn
作者简介:YANG Sheng-hui, Mobile: 18280872768, E-mail: yangshenghui_1013@163.com
基金资助:
This work was supported by the National 973 Program of China (2011CB100401), the Chongqing Municipal Science and Technology Research Project of China (2010AA1019), the National Science and Technology Key Projects of China (2009ZX08001-011B and 2009ZX08009-072B) and the National Science Fund for Distinguished Young Scholars of China (30825030).

Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice

YANG Sheng-hui, NIU Xiang-li, LUO Di, CHEN Chang-dong, YU Xu, TANG Wei, LU Bao-rong, LIU Yong-sheng

1.Key Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R.China
2.College of Life Sciences, Chongqing University, Chongqing 400044, P.R.China
3.Key Laboratory for Biodiversity Science and Ecological Engineering, Ministry of Education/Institute of Biodiversity Science, Fudan University, Shanghai 200433, P.R.China

Received:2011-04-28 Online:2012-09-01 Published:2012-09-09
Contact: Correspondence LIU Yong-sheng, Tel/Fax: +86-28-85460570, E-mail:liuyongsheng1122@yahoo.com.cn
About author:YANG Sheng-hui, Mobile: 18280872768, E-mail: yangshenghui_1013@163.com
Supported by:
This work was supported by the National 973 Program of China (2011CB100401), the Chongqing Municipal Science and Technology Research Project of China (2010AA1019), the National Science and Technology Key Projects of China (2009ZX08001-011B and 2009ZX08009-072B) and the National Science Fund for Distinguished Young Scholars of China (30825030).

摘要/Abstract

摘要： The aldehyde dehydrogenase (ALDH) superfamily of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an essential role in detoxification of reactive oxygen species (ROS) accumulated under the stressed conditions. In order to identify genes required for the stresses responses in the grass crop Oryza sativa, a homologue of ALDH gene (OsALDH22) was isolated and characterized. OsALDH22 is conserved in eukaryotes, shares high homology with the orthologs from aldehyde dehydrogenase subfamily ALDH22. The OsALDH22 encodes a protein of 597 amino acids that in plants exhibit high identity with the orthologs from Zea mays, Sorghum bicolor, Hordeum vulgare and Arabidopsis thaliana, respectively, and the conserved amino acid characteristics for ALDHs are present, including the possible NAD+ binding site (F-V-G-SP- G-V-G), the catalytic site (V-T-L-E-L-G-G-K) and the Cys active site. Semi-quantitative PCR and real-time PCR analysis indicates that OsALDH22 is expressed differentially in different tissues. Various elevated levels of OsALDH22 expression have been detected when the seedlings exposed to abiotic stresses including dehydration, high salinity and abscisic acid (ABA). Transgenic rice plants overexpressing OsALDH22 show elevated stresses tolerance. On the contrary, downregulation of OsALDH22 in the RNA interference (RNAi) repression transgenic lines manifests declined stresses tolerance.

关键词: rice (Oryza sativa), aldehyde dehydrogenase, abiotic stresses, stress tolerance

Abstract: The aldehyde dehydrogenase (ALDH) superfamily of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an essential role in detoxification of reactive oxygen species (ROS) accumulated under the stressed conditions. In order to identify genes required for the stresses responses in the grass crop Oryza sativa, a homologue of ALDH gene (OsALDH22) was isolated and characterized. OsALDH22 is conserved in eukaryotes, shares high homology with the orthologs from aldehyde dehydrogenase subfamily ALDH22. The OsALDH22 encodes a protein of 597 amino acids that in plants exhibit high identity with the orthologs from Zea mays, Sorghum bicolor, Hordeum vulgare and Arabidopsis thaliana, respectively, and the conserved amino acid characteristics for ALDHs are present, including the possible NAD+ binding site (F-V-G-SP- G-V-G), the catalytic site (V-T-L-E-L-G-G-K) and the Cys active site. Semi-quantitative PCR and real-time PCR analysis indicates that OsALDH22 is expressed differentially in different tissues. Various elevated levels of OsALDH22 expression have been detected when the seedlings exposed to abiotic stresses including dehydration, high salinity and abscisic acid (ABA). Transgenic rice plants overexpressing OsALDH22 show elevated stresses tolerance. On the contrary, downregulation of OsALDH22 in the RNA interference (RNAi) repression transgenic lines manifests declined stresses tolerance.

Key words: rice (Oryza sativa), aldehyde dehydrogenase, abiotic stresses, stress tolerance

YANG Sheng-hui, NIU Xiang-li, LUO Di, CHEN Chang-dong, YU Xu, TANG Wei, LU Bao-rong, LIU Yong-sheng. Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice[J]. Journal of Integrative Agriculture, 2012, 12(9): 1434-1444.

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Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice

Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice

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