Molecular and functional characterization of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Dunaliella salina

In green algae, the final step of the plastidial methylerythritol phosphate (MEP) pathway is catalyzed by 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR; EC: 1.17.1.2), an enzyme proposed to play a key role in the regulation of isoprenoid biosynthesis. Here we report the isolation and funct...

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Détails bibliographiques
Publié dans:Journal of plant physiology. - 1979. - 166(2009), 9 vom: 01. Juni, Seite 968-77
Auteur principal: Ramos, Ana A (Auteur)
Autres auteurs: Marques, Ana R, Rodrigues, Marta, Henriques, Nuno, Baumgartner, Alexandra, Castilho, Rita, Brenig, Bertram, Varela, João C
Format: Article en ligne
Langue:English
Publié: 2009
Accès à la collection:Journal of plant physiology
Sujets:Journal Article Research Support, Non-U.S. Gov't Algal Proteins DNA, Complementary Oxidoreductases EC 1.-
Description
Résumé:In green algae, the final step of the plastidial methylerythritol phosphate (MEP) pathway is catalyzed by 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR; EC: 1.17.1.2), an enzyme proposed to play a key role in the regulation of isoprenoid biosynthesis. Here we report the isolation and functional characterization of a 1959-bp Dunaliella salina HDR (DsHDR) cDNA encoding a deduced polypeptide of 474 amino acid residues. Phylogenetic analysis implied a cyanobacterial origin for plant and algal HDR genes. Steady-state DsHDR transcript levels were higher in D. salina cells submitted to nutritional depletion, high salt and/or high light, suggesting that DsHDR may respond to the same environmental cues as genes involved in carotenoid biosynthesis
Description:Date Completed 07.07.2009
Date Revised 30.09.2020
published: Print-Electronic
GENBANK: EG591728
Citation Status MEDLINE
ISSN:1618-1328
DOI:10.1016/j.jplph.2008.11.008