High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events
Many compounds produced by cyanobacteria act as serine protease inhibitors, such as the tetrapeptides aeruginosins (Aer), which are found widely distributed. The structural diversity of Aer is intriguingly high. However, the genetic basis of this remains elusive. In this study, we explored the genet...
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MDPI AG
2023-12-01
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author | Elisabeth Entfellner Kathrin B. L. Baumann Christine Edwards Rainer Kurmayer |
author_facet | Elisabeth Entfellner Kathrin B. L. Baumann Christine Edwards Rainer Kurmayer |
author_sort | Elisabeth Entfellner |
collection | DOAJ |
description | Many compounds produced by cyanobacteria act as serine protease inhibitors, such as the tetrapeptides aeruginosins (Aer), which are found widely distributed. The structural diversity of Aer is intriguingly high. However, the genetic basis of this remains elusive. In this study, we explored the genetic basis of Aer synthesis among the filamentous cyanobacteria <i>Planktothrix</i> spp. In total, 124 strains, isolated from diverse freshwater waterbodies, have been compared regarding variability within Aer biosynthesis genes and the consequences for structural diversity. The high structural variability could be explained by various recombination processes affecting Aer synthesis, above all, the acquisition of accessory enzymes involved in post synthesis modification of the Aer peptide (e.g., halogenases, glycosyltransferases, sulfotransferases) as well as a large-range recombination of Aer biosynthesis genes, probably transferred from the bloom-forming cyanobacterium <i>Microcystis</i>. The Aer structural composition differed between evolutionary <i>Planktothrix</i> lineages, adapted to either shallow or deep waterbodies of the temperate climatic zone. Thus, for the first time among bloom-forming cyanobacteria, chemical diversification of a peptide family related to eco-evolutionary diversification has been described. It is concluded that various Aer peptides resulting from the recombination event act in chemical defense, possibly as a replacement for microcystins. |
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spelling | doaj.art-9670ec03ca004147972f20fbbaaafe1e2023-12-22T14:22:24ZengMDPI AGMarine Drugs1660-33972023-12-01211263810.3390/md21120638High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination EventsElisabeth Entfellner0Kathrin B. L. Baumann1Christine Edwards2Rainer Kurmayer3Research Department for Limnology, Universität Innsbruck, Mondseestrasse 9, 5310 Mondsee, AustriaResearch Department for Limnology, Universität Innsbruck, Mondseestrasse 9, 5310 Mondsee, AustriaCyanoSol Research Group, Pharmacy & Life Sciences, Robert Gordon University, Aberdeen AB10 7GJ, UKResearch Department for Limnology, Universität Innsbruck, Mondseestrasse 9, 5310 Mondsee, AustriaMany compounds produced by cyanobacteria act as serine protease inhibitors, such as the tetrapeptides aeruginosins (Aer), which are found widely distributed. The structural diversity of Aer is intriguingly high. However, the genetic basis of this remains elusive. In this study, we explored the genetic basis of Aer synthesis among the filamentous cyanobacteria <i>Planktothrix</i> spp. In total, 124 strains, isolated from diverse freshwater waterbodies, have been compared regarding variability within Aer biosynthesis genes and the consequences for structural diversity. The high structural variability could be explained by various recombination processes affecting Aer synthesis, above all, the acquisition of accessory enzymes involved in post synthesis modification of the Aer peptide (e.g., halogenases, glycosyltransferases, sulfotransferases) as well as a large-range recombination of Aer biosynthesis genes, probably transferred from the bloom-forming cyanobacterium <i>Microcystis</i>. The Aer structural composition differed between evolutionary <i>Planktothrix</i> lineages, adapted to either shallow or deep waterbodies of the temperate climatic zone. Thus, for the first time among bloom-forming cyanobacteria, chemical diversification of a peptide family related to eco-evolutionary diversification has been described. It is concluded that various Aer peptides resulting from the recombination event act in chemical defense, possibly as a replacement for microcystins.https://www.mdpi.com/1660-3397/21/12/638horizontal gene transferchemical diversificationfreshwater ecotypesshallow waterbodiesdeep waterbodies |
spellingShingle | Elisabeth Entfellner Kathrin B. L. Baumann Christine Edwards Rainer Kurmayer High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events Marine Drugs horizontal gene transfer chemical diversification freshwater ecotypes shallow waterbodies deep waterbodies |
title | High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events |
title_full | High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events |
title_fullStr | High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events |
title_full_unstemmed | High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events |
title_short | High Structural Diversity of Aeruginosins in Bloom-Forming Cyanobacteria of the Genus <i>Planktothrix</i> as a Consequence of Multiple Recombination Events |
title_sort | high structural diversity of aeruginosins in bloom forming cyanobacteria of the genus i planktothrix i as a consequence of multiple recombination events |
topic | horizontal gene transfer chemical diversification freshwater ecotypes shallow waterbodies deep waterbodies |
url | https://www.mdpi.com/1660-3397/21/12/638 |
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