This site needs JavaScript to work properly. Please enable it to take advantage of the complete set of features!
Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

NIH NLM Logo
Log in
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2008 Mar;74(6):1791-7.
doi: 10.1128/AEM.02392-07. Epub 2008 Feb 1.

Microcyclamide biosynthesis in two strains of Microcystis aeruginosa: from structure to genes and vice versa

Affiliations

Microcyclamide biosynthesis in two strains of Microcystis aeruginosa: from structure to genes and vice versa

Nadine Ziemert et al. Appl Environ Microbiol. 2008 Mar.

Abstract

Comparative analysis of related biosynthetic gene clusters can provide new insights into the versatility of these pathways and allow the discovery of new natural products. The freshwater cyanobacterium Microcystis aeruginosa NIES298 produces the cytotoxic peptide microcyclamide. Here, we provide evidence that the cyclic hexapeptide is formed by a ribosomal pathway through the activity of a set of processing enzymes closely resembling those recently shown to be involved in patellamide biosynthesis in cyanobacterial symbionts of ascidians. Besides two subtilisin-type proteases and a heterocyclization enzyme, the gene cluster discovered in strain NIES298 encodes six further open reading frames, two of them without similarity to enzymes encoded by the patellamide gene cluster. Analyses of genomic data of a second cyanobacterial strain, M. aeruginosa PCC 7806, guided the discovery and structural elucidation of two novel peptides of the microcyclamide family. The identification of the microcyclamide biosynthetic genes provided an avenue by which to study the regulation of peptide synthesis at the transcriptional level. The precursor genes were strongly and constitutively expressed throughout the growth phase, excluding the autoinduction of these peptides, as has been observed for several peptide pheromone families in bacteria.

PubMed Disclaimer

Figures

FIG. 1.
FIG. 1.
Microcyclamide gene cluster in M. aeruginosa. (A) Schematic representation of the mca biosynthetic gene cluster in strains NIES298 and PCC 7806. Genes with similarity to patellamide biosynthesis genes in P. didemni are in gray. The precursor protein is highlighted in black. The light gray arrows represent ORFs that could not directly be assigned to microcyclamide biosynthesis. (B) McaE sequence of M. aeruginosa NIES298. The bold sequences show the product-coding sequences. The proposed start and stop cyclization sequences are underlined. The structure of microcyclamide from NIES298 is shown on the right. (C) McaE sequence. The bold sequences show the product-coding sequences. The proposed start and stop cyclization sequences are underlined. Predicted microcyclamide structures in PCC 7806 are shown below.
FIG. 2.
FIG. 2.
Structures of microcyclamides 7806A (peptide 1) and 7806B (peptide 2) from M. aeruginosa PCC 7806 as determined by NMR and MS analyses.
FIG. 3.
FIG. 3.
Transcription analysis of the mcaE precursor RNA from M. aeruginosa NIES298. Total RNA isolated from cells incubated under different light intensities and collected at different cell densities (OD, optical density at 750 nm). D, dark (0 μmol photons m−2 s−1); L, low light (16 μmol photons m−2 s−1); H, high light (68 μmol photons m−2 s−1); VH, very high light (180 μmol photons m−2 s−1). (A) Autoradiogram of DNA-RNA hybridization with an mcaE probe. (B) Agarose gel picture of the 16S rRNA stained with ethidium bromide under UV light. b, bases.

References

    1. Banker, R., and S. Carmeli. 1998. Tenuecyclamides A-D, cyclic hexapeptides from the cyanobacterium Nostoc spongiaeforme var. tenue. J. Nat. Prod. 61:1248-1251. - PubMed
    1. Blond, A., J. Peduzzi, C. Goulard, M. J. Chiuchiolo, M. Barthelemy, Y. Prigent, R. A. Salomon, R. N. Farias, F. Moreno, and S. Rebuffat. 1999. The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli. Eur. J. Biochem. 259:747-755. - PubMed
    1. Breukink, E. 2006. A lesson in efficient killing from two-component lantibiotics. Mol. Microbiol. 61:271-273. - PubMed
    1. Degnan, B. M., C. J. Hawkins, M. F. Lavin, E. J. McCaffrey, D. L. Parry, and D. J. Watters. 1989. Novel cytotoxic compounds from the ascidian Lissoclinum bistratum. J. Med. Chem. 32:1354-1359. - PubMed
    1. Delves-Broughton, J., P. Blackburn, R. J. Evans, and J. Hugenholtz. 1996. Applications of the bacteriocin, nisin. Antonie van Leeuwenhoek 69:193-202. - PubMed

Publication types

Associated data

LinkOut - more resources

Cite

AltStyle によって変換されたページ (->オリジナル) /