cDNA- derived identification of novel thionin precursors in VISCUM ALBUM that contain highly divergent thionin domains but conserved signal and acidic polypeptide domains |
Journal/Book: Plant Molecular Biol. 29, 1233-1242. 1993;
Abstract: The existence of new thionin variants in Viscum album has been deducedfrom cDNA sequences. Unlike the viscotoxins and related thioninspreviously found in different members of the Viscaceae, these novelthionins contain eight rather than six cysteine residues. In thisrespect they resemble thionins described previously from various cerealsand from Pyrularia pubera, which also contain eight cysteine residues atidentical positions. All of the new thionins of V. album are encoded ashigher-molecular-weight precursors consisting of a signal peptide, athionin domain and an acidic polypeptide domain. While the deduced aminoacid sequences of the thionin domains of different precursor moleculesare highly divergent, the two other domains are conserved among all ofthe variants and are distinct from the corresponding domains of thioninprecursors of other plant species. Author.
Keyword(s): AMINO-ACID-SEQUENCE
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