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Corrigendum for Tooming-Klunderud et al., Microbiology 153 (5) 1382-1393.
Microbiology 155 (2009), 2106-2108; DOI  10.1099/mic.0.30275-0IMMEDIATE OPEN ACCESS ARTICLE
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Microbiology 155 (2009), 2106-2108; DOI  10.1099/mic.0.30275-0
© 2009 Society for General Microbiology

Structural analysis of a non-ribosomal halogenated cyclic peptide and its putative operon from Microcystis: implication for evolution of cyanopeptolins

Ave Tooming-Klunderud, Thomas Rohrlack, Kamran Shalchian-Tabrizi, Tom Kristensen and Kjetill S. Jakobsen
Microbiology (2007), 153, part 5, 1382–1393

Due to a mistake during data processing, the putative substrate-binding pocket sequences of two of the adenylation domains were switched. Consequently, the structure of the peptide (cyanopeptolin-984) produced by Microcystis NIVA-CYA 172/5 (N-C 172/5) shown in Fig. 1Down is incorrect in the positioning of two amino acid residues. The underlying experimental data and the molecular mass of cyanopeptolin-984 were, however, correct. Fig. 1Down showing the corrected peptide structure and corrected Tables 1Down and 2Down are shown below. It should be noted that the phylogenetic tree of adenylation domain sequences (Fig. 3) is correct, but the designations for McnC1-Ile/Thr and McnE-Gln/Ile should have read McnC1-Gln/Thr and McnE-Ile, respectively. This correction makes interpretation of the phylogenetic tree more straightforward, and has no impact on the major conclusions of the paper.


Figure 1
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  		Fig. 1. (a) Molecular structure of cyanopeptolin-984 as deduced from LC/MS/MS fragmentation patterns. (b) Predicted structure of the peptide synthesized by the peptide synthetase from Microcystis N-C 172/5. R positions according to Namikoshi & Rinehart (1996)Down.

 

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  		Table 1. LC/MS/MS fragmentation pattern of cyanopeptolin-984 produced by Microcystis N-C 172/5

 

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  		Table 2. Deduced functions of encoded proteins in the mcn gene cluster of Microcystis N-C 172/5

 

REFERENCES

Challis, G. L., Ravel, J. & Townsend, C. A. (2000). Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem Biol 7, 211–224.[CrossRef][Medline]

Conti, E., Stachelhaus, T., Marahiel, M. A. & Brick, P. (1997). Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. EMBO J 16, 4174–4183.[CrossRef][Medline]

Namikoshi, M. & Rinehart, K. L. (1996). Bioactive compounds produced by cyanobacteria. J Ind Microbiol Biotechnol 17, 373–384.[CrossRef]

Rouhiainen, L., Paulin, L., Suomalainen, S., Hyytiäinen, H., Buikema, W., Haselkorn, R. & Sivonen, K. (2000). Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in Anabaena strain 90. Mol Microbiol 37, 156–167.[CrossRef][Medline]

Stachelhaus, T., Mootz, H. D. & Marahiel, M. A. (1999). The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem Biol 6, 493–505.[CrossRef][Medline]





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