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Published on May 12, 2006; 10.1104/pp.106.081091

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Received March 28, 2006
Returned for revision April 25, 2006
Accepted May 9, 2006

Early Steps in the Biosynthesis of NAD in Arabidopsis thaliana Start with Aspartate and Occur in the Plastid

Akira Katoh , Kazuya Uenohara , Mitsuru Akita , and Takashi Hashimoto *

Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan
Faculty of Agriculture, Ehime University, Matsuyama, Ehime 790-8566, Japan and Venture Business Laboratory, Ehime Univeristy, Matsuyama 790-8577, Japan

* Corresponding author; email: hasimoto{at}bs.naist.jp.

Nicotinamide adenine nucleotide (NAD) is a ubiquitous co-enzyme involved in oxidation-reduction reactions, and is synthesized by way of quinolinate. Animals and some bacteria synthesize quinolinate from tryptophan, whereas other bacteria synthesize quinolinate from aspartate using L-aspartate oxidase and quinolinate synthase. We show here that Arabidopsis thaliana uses the aspartate-to-quinolinate pathway. The Arabidopsis L-aspartate oxidase or quinolinate synthase gene complemented the E. coli mutant defective in the corresponding gene, and T-DNA-based disruption of either of these genes, as well as of the gene coding for the enzyme quinolinate phosphoribosyltransferase, was embryonic lethal. An analysis of functional green fluorescent protein-fused constructs and in vitro assays of uptake into isolated chloroplasts demonstrated that these three enzymes are located in the plastid.




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