The thionin family of antimicrobial peptides
Autor: | Holger Bohlmann, Tina Austerlitz, Timo Bohlmann, Katharina Höng |
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Rok vydání: | 2021 |
Předmět: |
Leaves
Plant Science Biochemistry chemistry.chemical_compound Amino Acids Flowering Plants Genetics 0303 health sciences Multidisciplinary biology Organic Compounds Plant Anatomy 030302 biochemistry & molecular biology Eukaryota Genomics Plants Chemistry Papaver Physical Sciences Medicine Transcriptome Analysis Research Article Pore Forming Cytotoxic Proteins Science Antimicrobial peptides Research and Analysis Methods Genome Complexity 03 medical and health sciences Selaginella Barley Gene family Sulfur Containing Amino Acids Amino Acid Sequence Cysteine Grasses Thionins Molecular Biology Techniques Molecular Biology 030304 developmental biology Cloning fungi Organic Chemistry Intron Chemical Compounds Organisms Biology and Life Sciences Proteins Computational Biology biology.organism_classification Genome Analysis Introns Thionin chemistry |
Zdroj: | PLoS ONE PLoS ONE, Vol 16, Iss 7, p e0254549 (2021) |
ISSN: | 1932-6203 |
Popis: | Thionins are antimicrobial peptides found only in plants. They are first produced as preproproteins and then processed to yield the usually 5 kDa, basic thionin peptide with three or four disulfide bridges. So far, thionins had only been found in some plant families of angiosperms. The One Thousand Plant Transcriptomes Initiative (1KP project) has sequenced the transcriptomes of more than 1000 plant species. We have used these data to search for new thionin sequences which gave 225 hits. After removing doublets these resulted in 133 new thionins. No sequences were found in algae and mosses. The phylogenetically earliest hits were from Selaginella species and from conifers. Many hits were from angiosperm plant families which were previously not known to contain thionins. A large gene family for thionins was found in Papaver. We isolated a genomic clone from Papaver somniferum which confirmed the general genomic structure with two small introns within the acidic domain. We also expressed the thionin encoded by the genomic clone and found that it had antimicrobial activity in vitro, especially against fungi. Previously, we had grouped thionins into four classes. The new data reported here led us to revise this classification. We now recognize only class 1 thionins with eight cysteine residues and class 2 thionins with six cysteine residues. The different variants that we found (and also previously known variants) can all be traced back to one of these two classes. Some of the variants had an uneven number of cysteine residues and it is not clear at the moment what that means for their threedimensional structure. |
Databáze: | OpenAIRE |
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