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Over‐expression of different aldehyde dehydrogenase genes in Arabidopsis thaliana confers tolerance to abiotic stress and protects plants against lipid peroxidation and oxidative stress
Author(s) -
KOTCHONI SIMEON O.,
KUHNS CHRISTINE,
DITZER ANDREA,
KIRCH HANSHUBERT,
BARTELS DOROTHEA
Publication year - 2006
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.2005.01458.x
Subject(s) - aldehyde dehydrogenase , arabidopsis thaliana , lipid peroxidation , abiotic stress , biochemistry , oxidative stress , biology , reactive oxygen species , transgene , mutant , arabidopsis , microbiology and biotechnology , gene , chemistry
Aldehyde dehydrogenases (ALDHs) play a major role in the detoxification processes of aldehydes generated in plants when exposed to abiotic stress. In previous studies, we have shown that the Arabidopsis thaliana ALDH3I1 gene is transcriptionally activated by abiotic stress, and over‐expression of the ALDH3I1 gene confers stress tolerance in transgenic plants. The A. thaliana genome contains 14 ALDH genes expressed in different sub‐cellular compartments and are presumably involved in different reactions. The purpose of this study was to compare the potential of a cytoplasmic and a chloroplastic stress‐inducible ALDH in conferring stress tolerance under different conditions. We demonstrated that constitutive or stress‐inducible expression of both the chloroplastic ALDH3I1 and the cytoplasmic ALDH7B4 confers tolerance to osmotic and oxidative stress. Stress tolerance in transgenic plants is accompanied by a reduction of H 2 O 2 and malondialdehyde (MDA) derived from cellular lipid peroxidation. Involvement of ALDHs in stress tolerance was corroborated by the analysis of ALDH3I1 and ALDH7B4 T‐DNA knockout (KO) mutants. Both mutant lines exhibited higher sensitivity to dehydration and salt than wild‐type (WT) plants. The results indicate that ALDH3I1 and ALDH7B4 not only function as aldehyde‐detoxifying enzymes, but also as efficient reactive oxygen species (ROS) scavengers and lipid peroxidation‐inhibiting enzymes. The potential of ALDHs to interfere with H 2 O 2 was also shown for recombinant bacterial proteins.