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Abstract Detail


Oxidative Stress

Shin, Jun-Hye [1], Kim, Sung-Ryul [2], An, Gynheung [2].

Functional Study of Aldehyde Dehydrogenase 7 (OsALDH7) in Rice (Oryza sativa L).

Aldehyde dehydrogenases (ALDH) are represented by a protein superfamily which catalyzes the irreversible oxidation of a wide range of reactive aldehydes to their corresponding carboxylic acids. In eukaryote, they are divided into more than 20 distinct protein families, which are ranged from substrate-specific enzymes to aldehyde dehydrogenases showing a highly variable substrate-specificity. In this poster, we report the function roles of OsALDH7 that belongs to family 7. OsALDH7 expression was detected in most organs and the transcript level was remarkably increased by oxidative and abiotic stresses such as submergence and dehydration treatment. Under a variety of stress conditions, osaldh7 null mutants were more sensitive to cold and high salt stresses and paraquat treatment. Upon the stress treatments, hydrogen peroxide (H2O2) levels were markedly increased in mutant plants compared to the wild-type. Likewise, the mutants also exhibited an enhanced sensitivity to lipid peroxidation. These results suggest that OsALDH7 may be involved in detoxification responses by removing aldehydes, which are formed by a variety of stress conditions. Interestingly, the mutant endosperms accumulated yellow-brown pigments, which are likely the reduction products of lipids, implying that OsALDH7 also functions in a metabolic pathway during seed development.


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1 - Pohang University of Science and Technology (POSTECH), Department of Life Science and National Research Laboratory of Plant Functional Genomics, Pohang, 790-784, Republic of Korea
2 - Pohang University of Science and Technology (POSTECH), Department of Life Science and National Research Laboratory of Plant Functional Genomics

Keywords:
ALDH
oxidative stress.

Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P06006
Abstract ID:271


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