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Báo cáo khoa học: Cloning, characterization and localization of a novel basic peroxidase gene from Catharanthus roseus

Catharanthus roseus(L.) G. Don produces a number of biologically active terpenoid indole alkaloids via a complex terpenoid indole alkaloid biosyn-thetic pathway. The final dimerization step of this pathway, leading to the synthesis of a dimeric alkaloid, vinblastine, was demonstrated to be cata-lyzed by a basic peroxidase. | ễFEBS Journal Cloning characterization and localization of a novel basic peroxidase gene from Catharanthus roseus Santosh Kumar Ajaswrata Dutta Alok K. Sinha and Jayanti Sen Nationalcentre for Plant Genome Research JNU Campus Aruna Asaf Ali Marg New Delhi India Keywords Catharanthus roseus organ specific peroxidase terpenoid indole alkaloid subcellular localization Correspondence A. K. Sinha National Centre for Plant Genome Research JNU Campus Aruna Asaf Ali Marg New Delhi 110 067 India Fax 91 11 26716658 Tel 91 11 26735188 E-mail alokksinha@yahoo.com Website http www.ncpgr.nic.in Note This paper is dedicated to the inspirational memory of Dr Jayanti Sen Received 1 December 2006 revised 2 January 2007 accepted 3 Januay 2007 doi 10.1111 j.1742-4658.2007.05677.x Catharanthus roseus L. G. Don produces a number of biologically active terpenoid indole alkaloids via a complex terpenoid indole alkaloid biosynthetic pathway. The final dimerization step of this pathway leading to the synthesis of a dimeric alkaloid vinblastine was demonstrated to be catalyzed by a basic peroxidase. However reports of the gene encoding this enzyme are scarce for C. roseus. We report here for the first time the cloning characterization and localization of a novel basic peroxidase CrPrx from C. roseus. A 394 bp partial peroxidase cDNA CrIntI was initially amplified from the internodal stem tissue using degenerate oligonucleotide primers and cloned. The full-length coding region of CrPrx cDNA was isolated by screening a leaf-specific cDNA library with CrIntI as probe. The CrPrx nucleotide sequence encodes a deduced translation product of 330 amino acids with a 21 amino acid signal peptide suggesting that CrPrx is secretory in nature. The molecular mass of this unprocessed and unmodified deduced protein is estimated to be 37.43 kDa and the pI value is 8.68. CrPrx was found to belong to a three intron category of gene that encodes a class III basic secretory peroxidase. CrPrx protein and mRNA .