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Published on December 7, 2007; 10.1104/pp.107.107060

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Received August 9, 2007
Accepted November 23, 2007

Molecular cloning and characterization of a vacuolar class III peroxidase involved in the metabolism of anticancer alkaloids in Catharanthus roseus (L.) G. Don

Maria Manuela R. Costa , Frederique Hilliou , Patricia Duarte , Luis Gustavo Pereira , Iolanda Almeida , Mark Leech , Johan Memelink , Alfonso Ros Barcelo , and Mariana Sottomayor *

John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK; IBMC – Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; Department of Botany of Faculty of Sciences, University of Porto, Rua do Campo Alegre, 1191, 4150-181 Porto, Portugal; Institute of Biology, University of Leiden, Clusius Laboratory, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands; Department of Plant Biology (Plant Physiology), University of Murcia, E-30100 Murcia, Spain

* Corresponding author; email: msottoma{at}ibmc.up.pt.

Catharanthus roseus produces low levels of two dimeric terpenoid indole alkaloids, vinblastine and vincristine, which are widely used in cancer chemotherapy. The dimerization reaction leading to {alpha}-3',4'-anhydrovinblastine is a key regulatory step for the production of the anticancer alkaloids in planta and has potential application in the industrial production of two semi-synthetic derivatives also used as anticancer drugs. In this work, we report the cloning, characterization and subcellular localization of an enzyme with anhydrovinblastine synthase activity identified as the major class III peroxidase present in C. roseus leaves and named CrPrx1. The deduced amino acid sequence corresponds to a polypeptide of 363 amino acids including an N-terminal signal peptide showing the secretory nature of CrPrx1. CrPrx1 has a two intron structure and is present as a single gene copy. Phylogenetic analysis indicates that CrPrx1 belongs to an evolutionary branch of vacuolar class III peroxidases whose members seem to have been recruited for different functions during evolution. Expression of a GFP-CrPrx1 fusion confirmed the vacuolar localization of this peroxidase, the exact subcellular localization of the alkaloid monomeric precursors and dimeric products. Expression data further supports the role of CrPrx1 in AVLB biosynthesis, indicating the potential of CrPrx1 as a target to increase alkaloid levels in the plant.




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