Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice
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...
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| Format: | Article |
| Language: | English |
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Elsevier
2012-09-01
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| Series: | Journal of Integrative Agriculture |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2095311912601439 |
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| author | Sheng-hui YANG Xiang-li NIU Di LUO Chang-dong CHEN Xu YU Wei TANG Bao-rong LU Yong-sheng LIU |
| author_facet | Sheng-hui YANG Xiang-li NIU Di LUO Chang-dong CHEN Xu YU Wei TANG Bao-rong LU Yong-sheng LIU |
| author_sort | Sheng-hui YANG |
| collection | DOAJ |
| description | 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-S-P-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, down-regulation of OsALDH22 in the RNA interference (RNAi) repression transgenic lines manifests declined stresses tolerance. |
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| id | doaj.art-da98d302ca1b41db8c8d32da65688792 |
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| issn | 2095-3119 |
| language | English |
| last_indexed | 2024-12-18T01:38:21Z |
| publishDate | 2012-09-01 |
| publisher | Elsevier |
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| series | Journal of Integrative Agriculture |
| spelling | doaj.art-da98d302ca1b41db8c8d32da656887922022-12-21T21:25:25ZengElsevierJournal of Integrative Agriculture2095-31192012-09-0111914341444Functional Characterization of an Aldehyde Dehydrogenase Homologue in RiceSheng-hui YANG0Xiang-li NIU1Di LUO2Chang-dong CHEN3Xu YU4Wei TANG5Bao-rong LU6Yong-sheng LIU7Key Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R. China; YANG Sheng-hui, Mobile: 18280872768College of Life Sciences, Chongqing University, Chongqing 400044, P.R. ChinaKey Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R. ChinaKey Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R. ChinaKey Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R. ChinaKey Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R. ChinaKey Laboratory for Biodiversity Science and Ecological Engineering, Ministry of Education/Institute of Biodiversity Science, Fudan University, Shanghai 200433, P.R. ChinaKey Laboratory for Bio-Resource and Eco-Environment, Minstry of Education/College of Life Sciences, Sichuan University, Chengdu 610064, P.R. China; College of Life Sciences, Chongqing University, Chongqing 400044, P.R. China; Correspondence LIU Yong-sheng, Tel/Fax: +86-28-85460570The 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-S-P-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, down-regulation of OsALDH22 in the RNA interference (RNAi) repression transgenic lines manifests declined stresses tolerance.http://www.sciencedirect.com/science/article/pii/S2095311912601439rice (Oryza sativa)aldehyde dehydrogenaseabiotic stressesstress tolerance |
| spellingShingle | Sheng-hui YANG Xiang-li NIU Di LUO Chang-dong CHEN Xu YU Wei TANG Bao-rong LU Yong-sheng LIU Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice Journal of Integrative Agriculture rice (Oryza sativa) aldehyde dehydrogenase abiotic stresses stress tolerance |
| title | Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice |
| title_full | Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice |
| title_fullStr | Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice |
| title_full_unstemmed | Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice |
| title_short | Functional Characterization of an Aldehyde Dehydrogenase Homologue in Rice |
| title_sort | functional characterization of an aldehyde dehydrogenase homologue in rice |
| topic | rice (Oryza sativa) aldehyde dehydrogenase abiotic stresses stress tolerance |
| url | http://www.sciencedirect.com/science/article/pii/S2095311912601439 |
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