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פותח על ידי קלירמאש פתרונות בע"מ -
TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato
Year:
1997
Source of publication :
Journal of Biological Chemistry
Authors :
פארן, אילן
;
.
Volume :
272
Co-Authors:
Orit, N., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Eshed, Y., Dept. of Field and Vegetable Crops, Otto Warburg Ctr. for Biotechnology, Hebrew University of Jerusalem, Rehovot 76100, Israel
Pinto, P., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Paran, I., Dept. of Field and Vegetable Crops, Otto Warburg Ctr. for Biotechnology, Hebrew University of Jerusalem, Rehovot 76100, Israel
Zamir, D., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Fluhr, R., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Facilitators :
From page:
1019
To page:
1025
(
Total pages:
7
)
Abstract:
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 (TA01). 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.
Note:
Related Files :
Animals
Base Sequence
chromosome mapping
gene mapping
hormone synthesis
nicotinamide adenine dinucleotide
plant growth
עוד תגיות
תוכן קשור
More details
DOI :
10.1074/jbc.272.2.1019
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29242
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:45
Scientific Publication
TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato
272
Orit, N., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Eshed, Y., Dept. of Field and Vegetable Crops, Otto Warburg Ctr. for Biotechnology, Hebrew University of Jerusalem, Rehovot 76100, Israel
Pinto, P., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Paran, I., Dept. of Field and Vegetable Crops, Otto Warburg Ctr. for Biotechnology, Hebrew University of Jerusalem, Rehovot 76100, Israel
Zamir, D., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
Fluhr, R., Department of Plant Genetics, Weizmann Institute of Science, P. O. Box 26, Rehovot, Israel
TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato
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 (TA01). 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.
Scientific Publication
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