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First published online September 4, 2003; 10.1104/pp.103.026609

Plant Physiology 133:794-802 (2003)
© 2003 American Society of Plant Biologists

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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

The Nitrilase ZmNIT2 Converts Indole-3-Acetonitrile to Indole-3-Acetic Acid1

Woong June Park2, Verena Kriechbaumer, Axel Müller, Markus Piotrowski, Robert B. Meeley, Alfons Gierl and Erich Glawischnig*

Lehrstuhl für Genetik, Technische Universität München, D–85350 Freising, Germany (W.J.P., V.K., A.G., E.G.); Lehrstuhl für Pflanzenphysiologie, Ruhr-Universität, D–44801 Bochum, Germany (A.M., M.P.); and Pioneer Hi-Bred International, Johnston, Iowa 50131–1004 (R.B.M.)

We isolated two nitrilase genes, ZmNIT1 and ZmNIT2, from maize (Zea mays) that share 75% sequence identity on the amino acid level. Despite the relatively high homology to Arabidopsis NIT4, ZmNIT2 shows no activity toward {beta}-cyano-alanine, the substrate of Arabidopsis NIT4, but instead hydrolyzes indole-3-acetonitrile (IAN) to indole-3-acetic acid (IAA). ZmNIT2 converts IAN to IAA at least seven to 20 times more efficiently than AtNIT1/2/3. Quantitative real-time polymerase chain reaction revealed the gene expression of both nitrilases in maize kernels where high concentrations of IAA are synthesized tryptophan dependently. Nitrilase protein and endogenous nitrilase activity are present in maize kernels together with the substrate IAN. These results suggest a role for ZmNIT2 in auxin biosynthesis.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.026609.

1 This work was supported by the Deutsche Forschungsgemeinschaft Schwerpunktprogramm 1067.

2 Present address: Department of Molecular Biology, Dankook University, Seoul 140–714, South-Korea.

* Corresponding author; e-mail egl{at}wzw.tum.de; fax 49–8161–71–5636.

Received May 8, 2003; returned for revision July 1, 2003; accepted July 8, 2003.


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