HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplementary figures Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Tooming-Klunderud, A. Articles by Jakobsen, K. S. Search for Related Content PubMed PubMed Citation Articles by Tooming-Klunderud, A. Articles by Jakobsen, K. S. Agricola Articles by Tooming-Klunderud, A. Articles by Jakobsen, K. S.

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

¹ Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway
² NIVA, Norwegian Institute for Water Research, 0411 Oslo, Norway
³ Department of Biology, Centre for Ecological and Evolutionary Synthesis (CEES), University of Oslo, 0316 Oslo, Norway

Correspondence
Kjetill S. Jakobsen
kjetill.jakobsen{at}bio.uio.no

The structure of the major peptide produced by Microcystis cf. wesenbergii NIVA-CYA 172/5, the halogenated heptapeptide cyanopeptolin-984, was determined using LC/MS/MS. A gene cluster encoding a peptide synthetase putatively producing a cyanopeptolin was cloned from the same strain and sequenced. The cluster consists of four genes encoding peptide synthetases and one gene encoding a halogenase. Two additional ORFs transcribed in the opposite direction were found in the 5' flanking sequence; one of these encodes an ABC transporter. The overall organization of the cyanopeptolin synthetase operon (mcn) resembles a previously analysed anabaenopeptilide synthetase operon (apd) from Anabaena strain 90. Phylogenetic analyses of the individual domains from Mcn, Apd and other cyanobacterial peptide synthetases showed clustering of the adenylation domains according to function irrespective of operon origin – indicating strong functional constraints across peptide synthetases. In contrast, the condensation and thiolation domains to a large extent grouped according to operon affiliation or position in the respective operons. Phylogenetic analyses of condensation domains indicated that N-terminal domains and domains that condense L-amino acids and D-amino acids, respectively, form three separate groups. Although recombination events are likely to be involved in the evolution of mcn, no clear evidence of genetic recombination between the two cyanopeptolin gene clusters was found. Within the genus Microcystis, microcystin and cyanopeptolin synthetases have an evolutionary history of genomic coexistence. However, the data indicated that the two classes of peptide synthetase gene clusters have evolved independently.

The GenBank/EMBL/DDBJ accession number for the cyanopeptolin synthetase gene cluster described in this paper is DQ075244.

Four supplementary figures are available with the online version of this paper.

This article has been cited by other articles:

				T. Kaneko, N. Nakajima, S. Okamoto, I. Suzuki, Y. Tanabe, M. Tamaoki, Y. Nakamura, F. Kasai, A. Watanabe, K. Kawashima, et al. Complete Genomic Structure of the Bloom-forming Toxic Cyanobacterium Microcystis aeruginosa NIES-843 DNA Res, January 11, 2008; (2008) dsm026v1. [Abstract] [Full Text] [PDF]

				T. B. Rounge, T. Rohrlack, A. Tooming-Klunderud, T. Kristensen, and K. S. Jakobsen Comparison of Cyanopeptolin Genes in Planktothrix, Microcystis, and Anabaena Strains: Evidence for Independent Evolution within Each Genus Appl. Envir. Microbiol., November 15, 2007; 73(22): 7322 - 7330. [Abstract] [Full Text] [PDF]