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

Journal Article

TitleMolecular and functional characterization of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Dunaliella salina.
Publication TypeJournal Article
AuthorsRamos, AA, Marques, AR, Rodrigues, M, Henriques, N, Baumgartner, A, Castilho, R, Brenig, B, Varela, J
Year of Publication2009
JournalJ Plant Physiol
Volume166
Issue9
Date Published2009 Jun 1
Pagination968-77
ISSN1618-1328
KeywordsAlgal Proteins, Amino Acid Sequence, Blotting, Northern, Chlorophyta, Cloning, Molecular, DNA, Complementary, Genetic Complementation Test, Molecular Sequence Data, Oxidoreductases, Phylogeny, Sequence Homology, Amino Acid
Abstract

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.

DOI10.1016/j.jplph.2008.11.008
Sapientia

http://www.ncbi.nlm.nih.gov/pubmed/19155093?dopt=Abstract

Alternate JournalJ. Plant Physiol.
PubMed ID19155093