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Cloning and functional expression in Escherichia coli of a cDNA encoding cardenolide 16'-O-glucohydrolase from Digitalis lanata Ehrh.
Framm, J J; Peterson, A; Thoeringer, C; Pangert, A; Hornung, E; Feussner, I; Luckner, M; Lindemann, P.
Plant Cell Physiol ; 41(11): 1293-8, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11092916

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.


Subject(s)
DNA, Complementary/genetics , Digitalis/genetics , Escherichia coli/genetics , Glucosidases/genetics , Plant Proteins , Plants, Medicinal , Plants, Toxic , 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
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