Plant Physiology Preview
Published on September 4, 2003; 10.1104/pp.103.026609
Received May 8, 2003
Returned for revision July 1, 2003
Accepted July 8, 2003
The Nitrilase ZmNIT2 Converts Indole-3-Acetonitrile to Indole-3-Acetic Acid
Woong June Park , 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.)
* Corresponding author; email: egl{at}wzw.tum.de.
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  -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.
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