Cyanobacteria frequently form mass developments in surface waters. Populations consist of strains that differ in the production of bioactive peptides, e.g. microcystins (MC) inhibiting protein phosphatases 1 and 2A and anabaenopeptins (APN) inhibiting carboxypeptidases. Forty-nine strains (18 green-pigmented (phycocyanin-rich) P. agardhii strains and 31 redpigmented (phycoerythrin-rich) P. rubescens strains) of the filamentous cyanobacterium Planktothrix (Anagnostidis et Komare´k) were analysed for their MC and APN net production rates. These rates were compared with (i) the pigmentation, (ii) the proportion of extra-and intracellular peptide concentrations and (iii) the cellular growth rates under standardized laboratory conditions. Excluding the strains lacking MC and APN, the MC and APN contents varied up to 14-fold and 12-fold, each. The variation in minimum and maximum peptide content (0.32-4.51 mg MC mg À1 dry weight; 0.85-10.32 mg APN mg À1 dry weight) exceeded the variation found for chlorophyll a (4.8-16.9 mg mg À1 dry weight). The extracellular proportions of MC (0-62%) and APN (0-58%) varied among strains, however, on average, proportions of extracellular MC and APN were low (MC: 8.8 AE (1 SE) 1.9%, APN: 8.4 AE 1.8%). Among all strains cellular growth rates showed a 5-fold variation (0.07-0.33 doublings of dry weight.day
À1) and were found independent of the pigmentation and the peptide net production rate. It is concluded that the MC and APN net production rate is not causally related to the cell-division cycle and the synthesis of highest amounts of MC and APN does not constrain cell division.Key words: cyanobacteria, cyanotoxins, freshwater phytoplankton, harmful algal bloom, growth rate, high performance liquid chromatography, Microcystis, water reservoir
IntroductionBecause of their frequent occurrence in fresh water, toxin-producing cyanobacteria are considered to be a general threat to drinking water quality (Codd et al., 1999; WHO, 2004). Many of the studies dealing with toxin production have focused on microcystins (MC), cyclic heptapeptides inhibiting eukaryotic proteinphosphatase 1 and 2A. MCs are synthesized via non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) assembled into large multifunctional proteins encoded by the mcy gene cluster (Tillett et al., 2000). , where D-MeAsp is the non-proteinogenic amino acid D-erythro--iso-aspartic acid (methyl aspartate), Mdha is N-methyl-dehydroalanine and Adda is a -amino acid with a C 10 -chain: (2S, 3S, 8S, 9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid. X and Z represent variable L-amino acids in positions 2 and 4, respectively (Carmichael, 1992). Similar to MCs, anabaenopeptins (APN) have been reported to inhibit protein phosphatase 1 (APN A and B; Gkelis et al., 2006) as well as proteases such as carboxypeptidase A (APN G and H, Itou et al., 1999). APNs contain six amino acids: five of them form a cyclic structure with a sixth amino acid that is attached. The pentapeptide moiety has the common struct...