Seed-derived defensins from Scots pine: structural and functional features.
Autor: | Shalovylo YI; Ukrainian National Forestry University, 103, Gen. Chuprynka, St., Lviv, 79057, Ukraine., Yusypovych YM; Ukrainian National Forestry University, 103, Gen. Chuprynka, St., Lviv, 79057, Ukraine., Hrunyk NI; Ukrainian National Forestry University, 103, Gen. Chuprynka, St., Lviv, 79057, Ukraine., Roman II; Ivan Franko National University of Lviv, 1, Saksagansky St., Lviv, 79005, Ukraine., Zaika VK; Ukrainian National Forestry University, 103, Gen. Chuprynka, St., Lviv, 79057, Ukraine., Krynytskyy HT; Ukrainian National Forestry University, 103, Gen. Chuprynka, St., Lviv, 79057, Ukraine., Nesmelova IV; University of North Carolina at Charlotte, 9201 University City Blvd., Charlotte, 28223, USA., Kovaleva VA; Ukrainian National Forestry University, 103, Gen. Chuprynka, St., Lviv, 79057, Ukraine. kovaleva@nltu.edu.ua. |
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Jazyk: | angličtina |
Zdroj: | Planta [Planta] 2021 Nov 24; Vol. 254 (6), pp. 129. Date of Electronic Publication: 2021 Nov 24. |
DOI: | 10.1007/s00425-021-03788-w |
Abstrakt: | Main Conclusion: The recombinant PsDef5.1 defensin inhibits the growth of phytopathogenic fungi, Gram-positive and Gram-negative bacteria, and human pathogen Candida albicans. Expression of seed-derived Scots pine defensins is tissue-specific and developmentally regulated. Plant defensins are ubiquitous antimicrobial peptides that possess a broad spectrum of activities and multi-functionality. The genes for these antimicrobial proteins form a multigenic family in the plant genome and are expressed in every organ. Most of the known defensins have been isolated from seeds of various monocot and dicot species, but seed-derived defensins have not yet been characterized in gymnosperms. This study presents the isolation of two new 249 bp cDNA sequences from Scots pine seeds with 97.9% nucleotide homology named PsDef5.1 and PsDef5.2. Their deduced amino acid sequences have typical plant defensin features, including an endoplasmic reticulum signal sequence of 31 amino acids (aa), followed by a characteristic defensin domain of 51 aa. To elucidate the functional activity of new defensins, we expressed the mature form of PsDef5.1 in a prokaryotic system. The purified recombinant peptide exhibited activity against the phytopathogenic fungi and Gram-negative and Gram-positive bacteria with the IC (© 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.) |
Databáze: | MEDLINE |
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