Molecular identification and characterization of the Arabidopsis delta(3,5),delta(2,4)-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the beta-oxidation cycle of unsaturated fatty acids.

Détails

ID Serval
serval:BIB_BBB3E2D698EC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Molecular identification and characterization of the Arabidopsis delta(3,5),delta(2,4)-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the beta-oxidation cycle of unsaturated fatty acids.
Périodique
Plant Physiology
Auteur(s)
Goepfert S., Vidoudez C., Rezzonico E., Hiltunen J.K., Poirier Y.
ISSN
0032-0889 (Print)
ISSN-L
0032-0889
Statut éditorial
Publié
Date de publication
2005
Volume
138
Numéro
4
Pages
1947-1956
Langue
anglais
Résumé
Degradation of unsaturated fatty acids through the peroxisomal beta-oxidation pathway requires the participation of auxiliary enzymes in addition to the enzymes of the core beta-oxidation cycle. The auxiliary enzyme delta(3,5),delta(2,4)-dienoyl-coenzyme A (CoA) isomerase has been well studied in yeast (Saccharomyces cerevisiae) and mammals, but no plant homolog had been identified and characterized at the biochemical or molecular level. A candidate gene (At5g43280) was identified in Arabidopsis (Arabidopsis thaliana) encoding a protein showing homology to the rat (Rattus norvegicus) delta(3,5),delta(2,4)-dienoyl-CoA isomerase, and possessing an enoyl-CoA hydratase/isomerase fingerprint as well as aspartic and glutamic residues shown to be important for catalytic activity of the mammalian enzyme. The protein, named AtDCI1, contains a peroxisome targeting sequence at the C terminus, and fusion of a fluorescent protein to AtDCI1 directed the chimeric protein to the peroxisome in onion (Allium cepa) cells. AtDCI1 expressed in Escherichia coli was shown to have delta(3,5),delta(2,4)-dienoyl-CoA isomerase activity in vitro. Furthermore, using the synthesis of polyhydroxyalkanoate in yeast peroxisomes as an analytical tool to study the beta-oxidation cycle, expression of AtDCI1 was shown to complement the yeast mutant deficient in the delta(3,5),delta(2,4)-dienoyl-CoA isomerase, thus showing that AtDCI1 is also appropriately targeted to the peroxisome in yeast and has delta(3,5),delta(2,4)-dienoyl-CoA isomerase activity in vivo. The AtDCI1 gene is expressed constitutively in several tissues, but expression is particularly induced during seed germination. Proteins showing high homology with AtDCI1 are found in gymnosperms as well as angiosperms belonging to the Monocotyledon or Dicotyledon classes.
Mots-clé
Amino Acid Sequence, Arabidopsis/enzymology, Carbon-Carbon Double Bond Isomerases/chemistry, Carbon-Carbon Double Bond Isomerases/metabolism, Fatty Acids, Unsaturated/metabolism, Gene Expression Regulation, Plant, Lipid Peroxidation, Molecular Sequence Data, Mutation, Sequence Alignment, Sequence Homology, Amino Acid
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 19:42
Dernière modification de la notice
20/08/2019 15:29
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