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Volume 272, Number 2, Issue of January 10, 1997 pp. 1019-1025
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

TAO1, a Representative of the Molybdenum Cofactor Containing Hydroxylases from Tomato

(Received for publication, August 2, 1996, and in revised form, October 23, 1996)

Naomi Ori Dagger , Yuval Eshed § , Patricia Pinto Dagger , Ilan Paran § , Dani Zamir Dagger and Robert Fluhr Dagger

From the Dagger  Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel and the § Department of Field and Vegetable Crops, The Faculty of Agriculture and The Otto Warburg Center for Biotechnology, The Hebrew University of Jerusalem, Rehovot 76100, Israel

Aldehyde oxidase and xanthine dehydrogenase are a group of ubiquitous hydroxylases, containing a molybdenum cofactor (MoCo) and two iron-sulfur groups. Plant aldehyde oxidase and xanthine dehydrogenase activities are involved in nitrogen metabolism and hormone biosynthesis, and their corresponding genes have not yet been isolated. Here we describe a new gene from tomato, which shows the characteristics of a MoCo containing hydroxylase. It shares sequence homology with xanthine dehydrogenases and aldehyde oxidases from various organisms, and similarly contains binding sites for two iron-sulfur centers and a molybdenum-binding region. However, it does not contain the xanthine dehydrogenase conserved sequences thought to be involved in NAD binding and in substrate specificity, and is likely to encode an aldehyde oxidase-type activity. This gene was designated tomato aldehyde oxidase 1 (TAO1). TAO1 belongs to a multigene family, whose members are shown to map to clusters on chromosomes 1 and 11. MoCo hydroxylase activity is shown to be recognized by antibodies raised against recombinant TAO1 polypeptides. Immunoblots reveal that TAO1 cross-reacting material is ubiquitously expressed in various organisms, and in plants it is mostly abundant in fruits and rapidly dividing tissues.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.