New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.

Nodularia spumigena is a filamentous diazotrophic cyanobacterium that forms blooms in brackish water bodies. This cyanobacterium produces linear and cyclic peptide protease inhibitors which are thought to be part of a chemical defense against grazers. Here we show that N. spumigena produces structur...

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Autores principales:	David P Fewer, Jouni Jokela, Eeva Paukku, Julia Österholm, Matti Wahlsten, Perttu Permi, Olli Aitio, Leo Rouhiainen, Gonzalo V Gomez-Saez, Kaarina Sivonen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e3ed0f8891e2490e86e9a0ad2fd1d6f5
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spelling	oai:doaj.org-article:e3ed0f8891e2490e86e9a0ad2fd1d6f52021-11-18T08:56:31ZNew structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.1932-620310.1371/journal.pone.0073618https://doaj.org/article/e3ed0f8891e2490e86e9a0ad2fd1d6f52013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24040002/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Nodularia spumigena is a filamentous diazotrophic cyanobacterium that forms blooms in brackish water bodies. This cyanobacterium produces linear and cyclic peptide protease inhibitors which are thought to be part of a chemical defense against grazers. Here we show that N. spumigena produces structurally novel members of the aeruginosin family of serine protease inhibitors. Extensive chemical analyses including NMR demonstrated that the aeruginosins are comprised of an N-terminal short fatty acid chain, L-Tyr, L-Choi and L-argininal and in some cases pentose sugar. The genome of N. spumigena CCY9414 contains a compact 18-kb aeruginosin gene cluster encoding a peptide synthetase with a reductive release mechanism which offloads the aeruginosins as reactive peptide aldehydes. Analysis of the aeruginosin and spumigin gene clusters revealed two different strategies for the incorporation of N-terminal protecting carboxylic acids. These results demonstrate that strains of N. spumigena produce aeruginosins and spumigins, two families of structurally similar linear peptide aldehydes using separate peptide synthetases. The aeruginosins were chemically diverse and we found 11 structural variants in 16 strains from the Baltic Sea and Australia. Our findings broaden the known structural diversity of the aeruginosin peptide family to include peptides with rare N-terminal short chain (C2-C10) fatty acid moieties.David P FewerJouni JokelaEeva PaukkuJulia ÖsterholmMatti WahlstenPerttu PermiOlli AitioLeo RouhiainenGonzalo V Gomez-SaezKaarina SivonenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e73618 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q David P Fewer Jouni Jokela Eeva Paukku Julia Österholm Matti Wahlsten Perttu Permi Olli Aitio Leo Rouhiainen Gonzalo V Gomez-Saez Kaarina Sivonen New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.
description	Nodularia spumigena is a filamentous diazotrophic cyanobacterium that forms blooms in brackish water bodies. This cyanobacterium produces linear and cyclic peptide protease inhibitors which are thought to be part of a chemical defense against grazers. Here we show that N. spumigena produces structurally novel members of the aeruginosin family of serine protease inhibitors. Extensive chemical analyses including NMR demonstrated that the aeruginosins are comprised of an N-terminal short fatty acid chain, L-Tyr, L-Choi and L-argininal and in some cases pentose sugar. The genome of N. spumigena CCY9414 contains a compact 18-kb aeruginosin gene cluster encoding a peptide synthetase with a reductive release mechanism which offloads the aeruginosins as reactive peptide aldehydes. Analysis of the aeruginosin and spumigin gene clusters revealed two different strategies for the incorporation of N-terminal protecting carboxylic acids. These results demonstrate that strains of N. spumigena produce aeruginosins and spumigins, two families of structurally similar linear peptide aldehydes using separate peptide synthetases. The aeruginosins were chemically diverse and we found 11 structural variants in 16 strains from the Baltic Sea and Australia. Our findings broaden the known structural diversity of the aeruginosin peptide family to include peptides with rare N-terminal short chain (C2-C10) fatty acid moieties.
format	article
author	David P Fewer Jouni Jokela Eeva Paukku Julia Österholm Matti Wahlsten Perttu Permi Olli Aitio Leo Rouhiainen Gonzalo V Gomez-Saez Kaarina Sivonen
author_facet	David P Fewer Jouni Jokela Eeva Paukku Julia Österholm Matti Wahlsten Perttu Permi Olli Aitio Leo Rouhiainen Gonzalo V Gomez-Saez Kaarina Sivonen
author_sort	David P Fewer
title	New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.
title_short	New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.
title_full	New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.
title_fullStr	New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.
title_full_unstemmed	New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.
title_sort	new structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium nodularia spumigena.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e3ed0f8891e2490e86e9a0ad2fd1d6f5
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New structural variants of aeruginosin produced by the toxic bloom forming cyanobacterium Nodularia spumigena.

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