1. Cloning and functional expression in Escherichia coli of a cDNA encoding cardenolide 16'-O-glucohydrolase from Digitalis lanata Ehrh.
- Author
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Framm JJ, Peterson A, Thoeringer C, Pangert A, Hornung E, Feussner I, Luckner M, and Lindemann P
- Subjects
- Amino Acid Sequence, Blotting, Northern, Cardenolides metabolism, Cloning, Molecular, DNA, Complementary chemistry, Digitalis enzymology, Gene Expression Regulation, Enzymologic, Glucosidases metabolism, Molecular Sequence Data, RNA, Messenger genetics, RNA, Messenger metabolism, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Tissue Distribution, DNA, Complementary genetics, Digitalis genetics, Escherichia coli genetics, Glucosidases genetics, Plant Proteins, Plants, Medicinal, Plants, Toxic
- Abstract
A clone of cardenolide 16'-O-glucohydrolase cDNA (CGH I) was obtained from Digitalis lanata which encodes a protein of 642 amino acids (calculated molecular mass 73.2 kDa). The amino acid sequence derived from CGH I showed high homology to a widely distributed family of beta-glucohydrolases (glycosyl hydrolases family 1). The recombinant CGH I protein produced in Escherichia coli had CGH I activity. CGH I mRNA was detected in leaves, flowers, stems and fruits of D. lanata.
- Published
- 2000
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