alexa Cloning and Functional Expression of Ζ-Carotene
ISSN: 2155-9821

Journal of Bioprocessing & Biotechniques
Open Access

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Research Article

Cloning and Functional Expression of Ζ-Carotene Desaturase, A Novel Carotenoid Biosynthesis Gene From Ficus Carica

González Villa T1,2*, Araya-Garay JM1, Feijoo-Siota L1, Veiga-Crespo P1,2 and Sánchez-Pérez A3
1Department of Microbiology, University of Santiago de Compostela, Spain
2School of Biotechnology, University of Santiago de Compostela, 15782 Santiago de Compostela, Spain
3Discipline of Physiology, Bosch Institute, University of Sydney, NSW 2006, Australia
Corresponding Author : González Villa
Department of Microbiology
University of Santiago de Compostela, Spain
Tel:
+34981592490
Fax: +34981592490
E-mail: [email protected]
Received April 10, 2012; Accepted July 05, 2012; Published July 29, 2012
Citation: González Villa T, Araya-Garay JM, Feijoo-Siota L, Veiga-Crespo P, Sánchez-Pérez A (2012) Cloning and Functional Expression of Ζ-Carotene Desaturase, A Novel Carotenoid Biosynthesis Gene From Ficus Carica. J Bioprocess Biotech 2:125. doi: 10.4172/2155-9821.1000125
Copyright: © 2012 González Villa T, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 

Abstract

 Carotene desaturation, an essential step in the carotenoid biosynthesis pathway, is catalyzed by two enzymes, phytoene desaturase (PDS) and ζ-carotene desaturase (zeta carotene desaturase, ZDS). Here we describe cloning and E. coli expression of zdsfc, a novel Ficus carica ζ-carotene desaturase catalyzing dehydrogenation of ζ-carotene into neurosporene and finally lycopene. The ζ-carotene desaturase (ZDS) gene was amplified from the fig tree  by rapid amplification of cDNA ends (RACE) and spanned a 1746 bp open reading frame (ORF), encoding a protein of 582 amino acid residues with a predicted molecular weight of 64kD. The N-terminal region of this polypeptide contained a putative transit sequence for plastid targeting. By phylogenetic and sequence analyses, zdsfc showed high homology with previously described ζ-carotene desaturases from higher plant species [1-4]. Additionally, sequence analysis revealed a high degree of conservation among plant ZDSs. The deduced ZDS protein, designated zdsfc, also contains an N-terminus dinucleotide-binding, followed by a conserved region identified in other carotene desaturase sequences. These data, taken together, confirm our cloned zdsfc as an integral part of the ZDS family of proteins.

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