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Journal of Bacteriology, July 1999, p. 4089-4097, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Nonribosomal Peptide Synthesis and Toxigenicity of Cyanobacteria

Brett A. Neilan,1,2,* Elke Dittmann,2 Leo Rouhiainen,3 R. Amanda Bass,1 Verena Schaub,2 Kaarina Sivonen,3 and Thomas Börner2

School of Microbiology and Immunology, The University of New South Wales, Sydney 2052, New South Wales, Australia1; Institute for Biology (Genetics), Humboldt University of Berlin, D-10115 Berlin, Germany2; and Department of Applied Chemistry and Microbiology, University of Helsinki, FIN-00014 Helsinki, Finland3

Received 14 December 1998/Accepted 21 April 1999

Nonribosomal peptide synthesis is achieved in prokaryotes and lower eukaryotes by the thiotemplate function of large, modular enzyme complexes known collectively as peptide synthetases. These and other multifunctional enzyme complexes, such as polyketide synthases, are of interest due to their use in unnatural-product or combinatorial biosynthesis (R. McDaniel, S. Ebert-Khosla, D. A. Hopwood, and C. Khosla, Science 262:1546-1557, 1993; T. Stachelhaus, A. Schneider, and M. A. Marahiel, Science 269:69-72, 1995). Most nonribosomal peptides from microorganisms are classified as secondary metabolites; that is, they rarely have a role in primary metabolism, growth, or reproduction but have evolved to somehow benefit the producing organisms. Cyanobacteria produce a myriad array of secondary metabolites, including alkaloids, polyketides, and nonribosomal peptides, some of which are potent toxins. This paper addresses the molecular genetic basis of nonribosomal peptide synthesis in diverse species of cyanobacteria. Amplification of peptide synthetase genes was achieved by use of degenerate primers directed to conserved functional motifs of these modular enzyme complexes. Specific detection of the gene cluster encoding the biosynthetic pathway of the cyanobacterial toxin microcystin was shown for both cultured and uncultured samples. Blot hybridizations, DNA amplifications, sequencing, and evolutionary analysis revealed a broad distribution of peptide synthetase gene orthologues in cyanobacteria. The results demonstrate a molecular approach to assessing preexpression microbial functional diversity in uncultured cyanobacteria. The nonribosomal peptide biosynthetic pathways detected may lead to the discovery and engineering of novel antibiotics, immunosuppressants, or antiviral agents.

* Corresponding author. Mailing address: School of Microbiology and Immunology, The University of New South Wales, Sydney 2052, NSW, Australia. Phone: 612 9385 3235. Fax: 612 9385 1591. E-mail: b.neilan{at}unsw.edu.au.

Journal of Bacteriology, July 1999, p. 4089-4097, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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