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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
A selenoprotein in the plant kingdom
Year:
2002
Source of publication :
Journal of Biological Chemistry
Authors :
איל, יורם
;
.
בן חיים, גוזל
;
.
פו, ליאן ה'
;
.
Volume :
277
Co-Authors:
Fu, L.-H., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel, Structural Biology and Biochemistry, Hospital for Sick Children, Toronto, Ont. M5G 1X8, Canada
Wang, X.-F., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Eyal, Y., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
She, Y.-M., Departments of Physics and Astronomy, Winnipeg, Man. R3T 2N2, Canada, Department of Chemistry, University of Manitoba, Winnipeg, Man. R3T 2N2, Canada
Donald, L.J., Dept. of Pomology, University of California, Davis, CA 95616, United States
Standing, K.G., Department of Chemistry, University of Manitoba, Winnipeg, Man. R3T 2N2, Canada
Ben-Hayyim, G., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Facilitators :
From page:
25983
To page:
25991
(
Total pages:
9
)
Abstract:
Selenoproteins that contain the rare amino acid selenocysteine in their primary structure have been identified in diverse organisms such as viruses, bacteria, archea, and mammals, but so far not in yeast or plants. Among the most thoroughly investigated families of selenoenzymes are the animal glutathione peroxidases (GPXs). In the last few years, genes encoding GPX-like homologues from Chlamydomonas and higher plants have been isolated, but, unlike the animal ones, all of them have cysteine (rather than selenocysteine) residues in their catalytic site. In all organisms investigated that contain selenoproteins, selenocysteine is encoded by a UGA opal codon, which is usually a stop codon. We report here that, in Chlamydomonas reinhardtii, the cDNA-cloned sequence of a GPX homologue contains an internal TGA codon in frame to the ATG. Specific mRNA expression, protein production, and enzyme activity are selenium-dependent. Sequence analysis of the peptides produced by proteolytic digestion, performed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), confirmed the presence of a selenocysteine residue at the predicted site and suggest its location in the mitochondria. Thus, our data present the first direct proof that a UGA opal codon is decoded in the plant kingdom to incorporate selenocysteine.
Note:
Related Files :
Animals
bacteria
Biochemistry
cloning
DNA
gene expression
RNA
Selenium
עוד תגיות
תוכן קשור
More details
DOI :
10.1074/jbc.M202912200
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23996
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:04
You may also be interested in
Scientific Publication
A selenoprotein in the plant kingdom
277
Fu, L.-H., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel, Structural Biology and Biochemistry, Hospital for Sick Children, Toronto, Ont. M5G 1X8, Canada
Wang, X.-F., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Eyal, Y., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
She, Y.-M., Departments of Physics and Astronomy, Winnipeg, Man. R3T 2N2, Canada, Department of Chemistry, University of Manitoba, Winnipeg, Man. R3T 2N2, Canada
Donald, L.J., Dept. of Pomology, University of California, Davis, CA 95616, United States
Standing, K.G., Department of Chemistry, University of Manitoba, Winnipeg, Man. R3T 2N2, Canada
Ben-Hayyim, G., Department of Fruit-Tree Breeding and Molecular Genetics, Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
A selenoprotein in the plant kingdom
Selenoproteins that contain the rare amino acid selenocysteine in their primary structure have been identified in diverse organisms such as viruses, bacteria, archea, and mammals, but so far not in yeast or plants. Among the most thoroughly investigated families of selenoenzymes are the animal glutathione peroxidases (GPXs). In the last few years, genes encoding GPX-like homologues from Chlamydomonas and higher plants have been isolated, but, unlike the animal ones, all of them have cysteine (rather than selenocysteine) residues in their catalytic site. In all organisms investigated that contain selenoproteins, selenocysteine is encoded by a UGA opal codon, which is usually a stop codon. We report here that, in Chlamydomonas reinhardtii, the cDNA-cloned sequence of a GPX homologue contains an internal TGA codon in frame to the ATG. Specific mRNA expression, protein production, and enzyme activity are selenium-dependent. Sequence analysis of the peptides produced by proteolytic digestion, performed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), confirmed the presence of a selenocysteine residue at the predicted site and suggest its location in the mitochondria. Thus, our data present the first direct proof that a UGA opal codon is decoded in the plant kingdom to incorporate selenocysteine.
Scientific Publication
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