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

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Abstract(s)

In green algae,the final step of the plastidial methylerythritol phosphate (MEP) pathway is catalyzed by 4-hydroxy-3-methylbut-2-enyldiphosphate reductase(HDR; EC: 1.17.1.2),an enzyme proposed to play a keyrole 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.

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Keywords

Carotenogenesis Dunaliella salina 4-Hydroxy-3-methylbut-2-enyldiphosphate reductase Isoprenoid biosynthesis Methylerythritol phosphate pathway

Citation

Ramos, A. A.; Marques, A. R.; Rodrigues, M.; Henriques, N.; Baumgartner, A.; Castilho, R.; Brenig, B.; Varela, J. C. Molecular and functional characterization of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Dunaliella salina, Journal of Plant Physiology, 166, 9, 968-977, 2009.

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