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Applied and Environmental Microbiology, April 2009, p. 2017-2026, Vol. 75, No. 7
0099-2240/09/$08.00+0 doi:10.1128/AEM.02258-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
Plasticity and Evolution of Aeruginosin Biosynthesis in Cyanobacteria
,
Keishi Ishida,1,2
Martin Welker,3,4,5*
Guntram Christiansen,1,6,7
Sabrina Cadel-Six,3
Christiane Bouchier,8
Elke Dittmann,1
Christian Hertweck,2 and
Nicole Tandeau de Marsac3
Institute of Biology, Humboldt Universität Berlin, 10115 Berlin, Germany,1 Leibniz Institute for Natural Product Research and Infection Biology (HKI), 07745 Jena, Germany,2 Institut Pasteur, Unité des Cyanobactéries, CNRS URA 2172, F75015 Paris, France,3 Institute of Chemistry, Technische Universität Berlin, 10587 Berlin, Germany,4 Anagnostec GmbH, 14476 Potsdam, Germany,5 Department of Chemistry, University of Hawaii at Manoa, Honolulu, Hawaii 96822,6 Institute of Limnology, Österreichische Akademie der Wissenschaften, 5310 Mondsee, Austria,7 Institut Pasteur, Pasteur Genopole Ile-de-France, F75015 Paris, France8
Received 1 October 2008/ Accepted 26 January 2009
Aeruginosins are bioactive oligopeptides that are produced in high structural diversity by strains of the bloom-forming cyanobacterial genera Microcystis and Planktothrix. A hallmark of aeruginosins is the unusual Choi moiety central to the tetrapeptides, while other positions are occupied by variable moieties in individual congeners. Here we report on three aeruginosin synthetase gene clusters (aer) of Microcystis aeruginosa (strains PCC 7806, NIES-98, and NIES-843). The analysis and comparison the aer gene clusters provide the first insight into the molecular basis of biosynthetic and structural plasticity in aeruginosin pathways. Major parts of the aer gene clusters are highly similar in all strains, particularly the genes coding for the first three nonribosomal peptide synthetase (NRPS) modules except for the region coding for the second adenylation domain. However, the gene clusters differ largely in genes coding for tailoring enzymes such as halogenases and sulfotransferases, reflecting structural peculiarities in aeruginosin congeners produced by the individual strains. Significant deviations were further observed in the C-terminal NRPS modules, suggesting two distinct release mechanisms. The architecture of the gene clusters is in agreement with the particular aeruginosin variants that are produced by individual strains, the structures of two of which (aeruginosins 686 A and 686 B) were elucidated. The aer gene clusters of Microcystis and Planktothrix are proposed to originate from a common ancestor and to have evolved to their present-day diversity largely through horizontal gene transfer and recombination events.
* Corresponding author. Present address: Department of Environmental Microbiology, FR 1-2, Technische Universität Berlin, 10587 Berlin, Germany. Phone: 49 30 31428626. Fax: 49 30 31473673. E-mail: martin.welker{at}tu-berlin.de
Published ahead of print on 5 February 2009.
Supplemental material for this article may be found at http://aem.asm.org/.
Applied and Environmental Microbiology, April 2009, p. 2017-2026, Vol. 75, No. 7
0099-2240/09/$08.00+0 doi:10.1128/AEM.02258-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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