Novel antifungal α-hairpinin peptide from Stellaria media seeds: structure, biosynthesis, gene structure and evolution

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• 作者：Anna A. Slavokhotova (1) <br> Eugene A. Rogozhin (2) <br> Alexander K. Musolyamov (2) <br> Yaroslav A. Andreev (2) <br> Peter B. Oparin (2) <br> Antonina A. Berkut (2) <br> Alexander A. Vassilevski (2) <br> Tsezi A. Egorov (2) <br> Eugene V. Grishin (2) <br> Tatyana I. Odintsova (1) <br>
• 关键词：Weeds ; cDNA cloning ; Gene structure ; Plant defense ; Protein biosynthesis ; α ; hairpinin
• 刊名：Plant Molecular Biology
• 出版年：2014
• 出版时间：January 2014
• 年：2014
• 卷：84
• 期：1-2
• 页码：189-202
• 全文大小：
• 作者单位：Anna A. Slavokhotova (1) <br> Eugene A. Rogozhin (2) <br> Alexander K. Musolyamov (2) <br> Yaroslav A. Andreev (2) <br> Peter B. Oparin (2) <br> Antonina A. Berkut (2) <br> Alexander A. Vassilevski (2) <br> Tsezi A. Egorov (2) <br> Eugene V. Grishin (2) <br> Tatyana I. Odintsova (1) <br><br>1. Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, 119991, Moscow, Russian Federation <br> 2. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russian Federation <br>
• ISSN：1573-5028

文摘

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 (C1X3b>C2Xnb>C3X3b>C4), 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 C1–C4 and C2–C3. 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.