In this work, we isolated and characterized novel antifungal proteins from seeds of dandelion (Taraxacum officinale Wigg.). We showed that they are represented by five isoforms, each consisting of two disulphide-bonded large and small subunits.
View Article and Find Full Text PDFTwo forms of a novel antimicrobial peptide (AMP), named WAMP-1a and WAMP-1b, that differ by a single C-terminal amino acid residue and belong to a new structural type of plant AMP were purified from seeds of Triticum kiharae Dorof. et Migusch. Although WAMP-1a and WAMP-1b share similarity with hevein-type peptides, they possess 10 cysteine residues arranged in a unique cysteine motif which is distinct from those described previously for plant AMPs, but is characteristic of the chitin-binding domains of cereal class I chitinases.
View Article and Find Full Text PDFThe origin of polyploid wheat genomes has been the subject of numerous studies and is the key problem in wheat phylogeny. Different diploid species have been supposed to donate genomes to tetraploid and hexaploid wheat species. To shed light on phylogenetic relationships between the presumable A genome donors and hexaploid wheat species we have applied a new approach: the comparison of defensins from diploid Triticum species, Triticum boeoticum Boiss.
View Article and Find Full Text PDFTen new defensins have been isolated from seeds of Triticum kiharae and related species of the Triticum and Aegilops genera by a combination of chromatographic procedures including affinity-, size-exclusion, and reversed-phase high-performance liquid chromatography. Nine were completely sequenced and shown to represent a family of closely related peptides with highly conserved amino acid sequences. Analysis of defensin compositions in diploid A-, B-, and D-genome donors to polyploid wheat allowed us for the first time to assign most defensin-encoding genes to particular hexaploid wheat genomes.
View Article and Find Full Text PDFFrom seeds of Triticum kiharae Dorof. et Migusch., 24 novel anti-microbial peptides were isolated and characterized by a combination of three-step HPLC (affinity, size-exclusion and reversed-phase) with matrix-assisted laser-desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry and Edman degradation.
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