Journal Article
| Título | Molecular and functional characterization of a cDNA encoding 4-hydroxy-3-methylbut-2-enyl diphosphate reductase from Dunaliella salina. |
| Publication Type | Journal Article |
| Authors | Ramos, AA, Marques, AR, Rodrigues, M, Henriques, N, Baumgartner, A, Castilho, R, Brenig, B, Varela, J |
| Year of Publication | 2009 |
| Journal | J Plant Physiol |
| Volume | 166 |
| Questão | 9 |
| Date Published | 2009 Jun 1 |
| Pagination | 968-77 |
| ISSN | 1618-1328 |
| Palavras-chave | Algal 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. |
| DOI | 10.1016/j.jplph.2008.11.008 |
| Sapientia | |
| Alternate Journal | J. Plant Physiol. |
| PubMed ID | 19155093 |
