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Cyanochelins, an overlooked class of widely distributed cyanobacterial siderophores, discovered by silent gene cluster awakening.
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SYSNO ASEP 0552516 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Cyanochelins, an overlooked class of widely distributed cyanobacterial siderophores, discovered by silent gene cluster awakening. Author(s) Galica, T. (CZ)
Borbone, N. (IT)
Mareš, Jan (BC-A) RID, ORCID
Kust, Andreja (BC-A) RID, ORCID
Caso, A. (IT)
Esposito, G. (IT)
Saurav, K. (CZ)
Hajek, J. (CZ)
Řeháková, Klára (BC-A) RID, ORCID
Urajová, P. (CZ)
Costantino, V. (IT)
Hrouzek, P. (CZ)Number of authors 12 Article number e03128-20 Source Title Applied and Environmental Microbiology. - : American Society for Microbiology - ISSN 0099-2240
Roč. 87, č. 17 (2021)Number of pages 13 s. Language eng - English Country US - United States Keywords cyanobacteria ; iron acquisition ; lipopeptides ; secondary metabolism ; siderophores Subject RIV EE - Microbiology, Virology OECD category Microbiology Method of publishing Limited access Institutional support BC-A - RVO:60077344 UT WOS 000693759300028 EID SCOPUS 85114119775 DOI 10.1128/AEM.03128-20 Annotation Cyanobacteria require iron for growth and often inhabit iron-limited habitats, yet only a few siderophores are known to be produced by them. We report that cyanobacterial genomes frequently encode polyketide synthase (PKS)/nonribosomal peptide synthetase (NRPS) biosynthetic pathways for synthesis of lipopeptides featuring beta-hydroxyaspartate (beta-OH-Asp), a residue known to be involved in iron chelation. Iron starvation triggered the synthesis of beta-OH-Asp lipopeptides in the cyanobacteria Rivularia sp. strain PCC 7116, Leptolyngbya sp. strain NIES-3755, and Rubidibacter lacunae strain KORDI 51-2. The induced compounds were confirmed to bind iron by mass spectrometry (MS) and were capable of Fe3+ to Fe2+ photoreduction, accompanied by their cleavage, when exposed to sunlight. The siderophore from Rivularia, named cyanochelin A, was structurally characterized by MS and nuclear magnetic resonance (NMR) and found to contain a hydrophobic tail bound to phenolate and oxazole moieties followed by five amino acids, including two modified aspartate residues for iron chelation. Phylogenomic analysis revealed 26 additional cyanochelin-like gene clusters across a broad range of cyanobacterial lineages. Our data suggest that cyanochelins and related compounds are widespread beta-OH-Asp-featuring cyanobacterial siderophores produced by phylogenetically distant species upon iron starvation. Production of photolabile siderophores by phototrophic cyanobacteria raises questions about whether the compounds facilitate iron monopolization by the producer or, rather, provide Fe2+ for the whole microbial community via photoreduction. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2022 Electronic address https://doi.org/10.1128/AEM.03128-20
Number of the records: 1