Novel antifungal α-hairpinin peptide from Stellaria media seeds: structure, biosynthesis, gene structure and evolution
| Autor: | Tatyana I. Odintsova, Yaroslav A. Andreev, Antonina A. Berkut, Tsezi A. Egorov, Eugene V. Grishin, Alexander A. Vassilevski, A. K. Musolyamov, Eugene A. Rogozhin, Peter B. Oparin, Anna A. Slavokhotova |
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| Rok vydání: | 2013 |
| Předmět: |
Antifungal Agents
Pseudogene Molecular Sequence Data Stellaria Peptide Plant Science Biology Homology (biology) Evolution Molecular food Tandem repeat Gene Expression Regulation Plant Complementary DNA Stellaria media Botany Genetics Amino Acid Sequence Cloning Molecular Gene Peptide sequence Plant Proteins chemistry.chemical_classification Fungi General Medicine food.food Biochemistry chemistry Seeds Agronomy and Crop Science |
| Zdroj: | Plant Molecular Biology. 84:189-202 |
| ISSN: | 1573-5028 0167-4412 |
| Popis: | Plant defense against disease is a complex multistage system involving initial recognition of the invading pathogen, signal transduction and activation of specialized genes. An important role in pathogen deterrence belongs to so-called plant defense peptides, small polypeptide molecules that present antimicrobial properties. Using multidimensional liquid chromatography, we isolated a novel antifungal peptide named Sm-AMP-X (33 residues) from the common chickweed (Stellaria media) seeds. The peptide sequence shows no homology to any previously described proteins. The peculiar cysteine arrangement (C(1)X3C(2)XnC(3)X3C(4)), however, allocates Sm-AMP-X to the recently acknowledged α-hairpinin family of plant defense peptides that share the helix-loop-helix fold stabilized by two disulfide bridges C(1)-C(4) and C(2)-C(3). Sm-AMP-X exhibits high broad-spectrum activity against fungal phytopathogens. We further showed that the N- and C-terminal "tail" regions of the peptide are important for both its structure and activity. The truncated variants Sm-AMP-X1 with both disulfide bonds preserved and Sm-AMP-X2 with only the internal S-S-bond left were progressively less active against fungi and presented largely disordered structure as opposed to the predominantly helical conformation of the full-length antifungal peptide. cDNA and gene cloning revealed that Sm-AMP-X is processed from a unique multimodular precursor protein that contains as many as 12 tandem repeats of α-hairpinin-like peptides. Structure of the sm-amp-x gene and two related pseudogenes sm-amp-x-ψ1 and sm-amp-x-ψ2 allows tracing the evolutionary scenario that led to generation of such a sophisticated precursor protein. Sm-AMP-X is a new promising candidate for engineering disease resistance in plants. |
| Databáze: | OpenAIRE |
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