Näytä suppeat kuvailutiedot

dc.contributor.authorMareš, Jan
dc.contributor.authorHájek, Jan
dc.contributor.authorUrajová, Petra
dc.contributor.authorKust, Andreja
dc.contributor.authorJokela, Jouni
dc.contributor.authorSaurav, Kumar
dc.contributor.authorGalica, Tomáš
dc.contributor.authorČapková, Kateřina
dc.contributor.authorMattila, Antti
dc.contributor.authorHaapaniemi, Esa
dc.contributor.authorPermi, Perttu
dc.contributor.authorMysterud, Ivar
dc.contributor.authorSkulberg, Olav M.
dc.contributor.authorKarlsen, Jan
dc.contributor.authorFewer, David P.
dc.contributor.authorSivonen, Kaarina
dc.contributor.authorTønnesen, Hanne Hjorth
dc.contributor.authorHrouzek, Pavel
dc.date.accessioned2019-02-20T10:19:02Z
dc.date.available2019-08-06T21:35:38Z
dc.date.issued2019
dc.identifier.citationMareš, J., Hájek, J., Urajová, P., Kust, A., Jokela, J., Saurav, K., Galica, T., Čapková, K., Mattila, A., Haapaniemi, E., Permi, P., Mysterud, I., Skulberg, O. M., Karlsen, J., Fewer, D. P., Sivonen, K., Tønnesen, H. H., & Hrouzek, P. (2019). Alternative biosynthetic starter units enhance the structural diversity of cyanobacterial lipopeptides. <i>Applied and Environmental Microbiology</i>, <i>85</i>(4), Article e02675-18. <a href="https://doi.org/10.1128/AEM.02675-18" target="_blank">https://doi.org/10.1128/AEM.02675-18</a>
dc.identifier.otherCONVID_28765121
dc.identifier.otherTUTKAID_79770
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/62888
dc.description.abstractPuwainaphycins (PUWs) and minutissamides (MINs) are structurally analogous cyclic lipopeptides possessing cytotoxic activity. Both types of compound exhibit high structural variability, particularly in the fatty acid (FA) moiety. Although a biosynthetic gene cluster responsible for synthesis of several PUW variants has been proposed in a cyanobacterial strain, the genetic background for MINs remains unexplored. Herein, we report PUW/MIN biosynthetic gene clusters and structural variants from six cyanobacterial strains. Comparison of biosynthetic gene clusters indicates a common origin of the PUW/MIN hybrid nonribosomal peptide synthetase and polyketide synthase. Surprisingly, the biosynthetic gene clusters encode two alternative biosynthetic starter modules, and analysis of structural variants suggests that initiation by each of the starter modules results in lipopeptides of differing lengths and FA substitutions. Among additional modifications of the FA chain, chlorination of minutissamide D was explained by the presence of a putative halogenase gene in the PUW/MIN gene cluster of Anabaena minutissima strain UTEX B 1613. We detected PUW variants bearing an acetyl substitution in Symplocastrum muelleri strain NIVA-CYA 644, consistent with an O-acetyltransferase gene in its biosynthetic gene cluster. The major lipopeptide variants did not exhibit any significant antibacterial activity, and only the PUW F variant was moderately active against yeast, consistent with previously published data suggesting that PUWs/MINs interact preferentially with eukaryotic plasma membranes. IMPORTANCE Herein, we deciphered the most important biosynthetic traits of a prominent group of bioactive lipopeptides. We reveal evidence for initiation of biosynthesis by two alternative starter units hardwired directly in the same gene cluster, eventually resulting in the production of a remarkable range of lipopeptide variants. We identified several unusual tailoring genes potentially involved in modifying the fatty acid chain. Careful characterization of these biosynthetic gene clusters and their diverse products could provide important insight into lipopeptide biosynthesis in prokaryotes. Some of the variants identified exhibit cytotoxic and antifungal properties, and some are associated with a toxigenic biofilm-forming strain. The findings may prove valuable to researchers in the fields of natural product discovery and toxicology.fi
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherAmerican Society for Microbiology
dc.relation.ispartofseriesApplied and Environmental Microbiology
dc.rightsIn Copyright
dc.subject.otherbiosynteesifi
dc.subject.otherpeptiditfi
dc.subject.othersyanobakteeritfi
dc.subject.otherbiosynthesisfi
dc.subject.otherpeptidesfi
dc.subject.othercyanobacteriafi
dc.titleAlternative biosynthetic starter units enhance the structural diversity of cyanobacterial lipopeptides
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201902061446
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineOrgaaninen kemiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineOrganic Chemistryen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2019-02-06T13:15:11Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn0099-2240
dc.relation.numberinseries4
dc.relation.volume85
dc.type.versionacceptedVersion
dc.rights.copyright© 2019 American Society for Microbiology
dc.rights.accesslevelopenAccessfi
dc.subject.ysobiosynteesi
dc.subject.ysopeptidit
dc.subject.ysosyanobakteerit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p14405
jyx.subject.urihttp://www.yso.fi/onto/yso/p15258
jyx.subject.urihttp://www.yso.fi/onto/yso/p3324
dc.rights.urlhttp://rightsstatements.org/page/InC/1.0/?language=en
dc.relation.doi10.1128/AEM.02675-18
dc.type.okmA1


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