Toxicity of Free Proline Revealed in an Arabidopsis T-DNA-Tagged Mutant Deficient in Proline Dehydrogenase
Author(s) -
Tokihiko Nanjo,
Miki Fujita,
Motoaki Seki,
Tomohiko Kato,
Satoshi Tabata,
Kazuo Shinozaki
Publication year - 2003
Publication title -
plant and cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.975
H-Index - 152
eISSN - 1471-9053
pISSN - 0032-0781
DOI - 10.1093/pcp/pcg066
Subject(s) - arabidopsis , proline dehydrogenase , mutant , proline , toxicity , biochemistry , biology , dehydrogenase , arabidopsis thaliana , complementary dna , enzyme , wild type , gene , microbiology and biotechnology , chemistry , amino acid , organic chemistry
The toxicity of proline (Pro) to plant growth has raised questions despite its protective functions in response to environmental stresses. To evaluate Pro toxicity, we isolated an Arabidopsis T-DNA-tagged mutant, pdh, that had a defect in Pro dehydrogenase (AtProDH), which catalyzes the first step of Pro catabolism. The pdh mutant showed hypersensitivity to exogenous application of < or =10 mM L-Pro, at which wild-type plants grew normally. A dose-dependent increase in internal free Pro accumulation was observed in pdh plants during external Pro supply. These results do not just prove the toxicity of Pro, but also suggest that AtProDH is the only enzyme acting as a functional ProDH in Arabidopsis: To further analyze the targets of Pro toxicity, we compared the expression of thousands of genes by pdh plants with that by wild-type plants by cDNA microarray analysis. Most genes were unaffected. Here we demonstrate Pro toxicity by using the pdh mutant and discuss a cause-and-effect action between an excess of free Pro and growth inhibition in Arabidopsis.
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