Nucleotide sequence of a cDNA encoding the vacuolar protein strictosidine synthase from Catharanthus roseus

• Published in: Nucleic acids research Vol. 18; no. 16; p. 4939
• Main Authors: McKnight, T D, Roessner, C A, Devagupta, R, Scott, A I, Nessler, C L
• Format: Journal Article
• Language: English
• Published: England 25.08.1990
• Subjects: alkaloids; Amino Acid Sequence; Base Sequence; Carbon-Nitrogen Lyases; Catharanthus roseus; DNA - genetics; genes; Molecular Sequence Data; Plants - enzymology; Plants - genetics; Sequence Homology, Nucleic Acid; Transferases - genetics; Vacuoles - enzymology
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/18.16.4939

Strictosidine synthase is a plant vacuolar glycoprotein that catalyses the condensation of tryptamine and secologanin to form strictosidine, a key intermediate in indole-type alkaloid production. Catharanthus roseus (Madagascar periwinkle) produces two clinically useful antitumor alkaloids, vinblastine and vincristine, derived from strictosidine. We used a labeled oligonucleotide derived from the sequence of the Rauwolfia serpentina strictosidine synthase gene to probe a C. roseus cDNA library. The translated region begins with two Met codons, the second of which is found within the Kozak consensus motif. The predicted amino acid sequences of both strictosidine synthases are 344 residues long and 274 (80%) of these positions are identical. The C. roseus strictosidine synthase signal peptide is unusual in that it does not contain a basic amino acid, as is usually found in signal peptides.