Biosynthesis of sideramines in fungi. Fusigen synthetase from extracts of <i>Fusarium cubense</i>

Anke, Heidrun; Anke, Timm; Diekmann, H.

doi:10.1016/0014-5793(73)80401-6

Cited by 19 publications

(9 citation statements)

References 14 publications

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“…This mechanism has been supported by biochemical data where hydroxyornithine-ATP-PP i exchange activity was observed in extracts prepared from ornithine hydroxamate siderophore-producing fungi (4,5). The genetic and molecular data presented herein indicate that sid2 is essential for ferrichrome biosynthesis.…”

Section: Discussionsupporting

confidence: 73%

Characterization of theUstilago maydis sid2Gene, Encoding a Multidomain Peptide Synthetase in the Ferrichrome Biosynthetic Gene Cluster

et al. 2001

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Ustilago maydis, the causal agent of corn smut disease, acquires and transports ferric ion by producing the extracellular, cyclic peptide, hydroxamate siderophores ferrichrome and ferrichrome A. Ferrichrome biosynthesis likely proceeds by hydroxylation and acetylation of L-ornithine, and later steps likely involve covalently bound thioester intermediates on a multimodular, nonribosomal peptide synthetase. sid1 encodes L-ornithine N 5 -oxygenase, which catalyzes hydroxylation of L-ornithine, the first committed step of ferrichrome and ferrichrome A biosynthesis in U. maydis. In this report we characterize sid2, another biosynthetic gene in the pathway, by gene complementation, gene replacement, DNA sequence, and Northern hybridization analysis. Nucleotide sequencing has revealed that sid2 is located 3.7 kb upstream of sid1 and encodes an intronless polypeptide of 3,947 amino acids with three iterated modules of an approximate length of 1,000 amino acids each. Multiple motifs characteristic of the nonribosomal peptide synthetase protein family were identified in each module. A corresponding iron-regulated sid2 transcript of 11 kb was detected by Northern hybridization analysis. By contrast, constitutive accumulation of this large transcript was observed in a mutant carrying a disruption of urbs1, a zinc finger, GATA family transcription factor previously shown to regulate siderophore biosynthesis in Ustilago. Multiple GATA motifs are present in the intergenic region between sid1 and sid2, suggesting bidirectional transcription regulation by urbs1 of this pathway. Indeed, mutation of two of these motifs, known to be important to regulation of sid1, altered the differential regulation of sid2 by iron.

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Section: Discussionsupporting

confidence: 73%

Characterization of theUstilago maydis sid2Gene, Encoding a Multidomain Peptide Synthetase in the Ferrichrome Biosynthetic Gene Cluster

et al. 2001

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“…Fusigen synthetase is an enzyme of 600±800 kDa and a pH optimum of 7.0 [66]. Its substrate is activated N 5 -cis-anhydromevalonyl-N 5 -hydroxy-Lornithine [67]. Since no dimers and trimers are found, the cyclic triester is presumably synthesized from monomers bound to the enzyme as adenylates or thioesters.…”

Section: Siderophores Containing Oligopeptidesmentioning

confidence: 99%

Peptide siderophores

1998

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Siderophores are low molecular weight iron chelators, produced by virtually all bacteria, fungi and some plants. They serve to deliver the essential element iron, barely soluble under aerobic conditions, into microbial cells. Siderophores are therefore important secondary metabolites which are very often based on amino acids and their derivatives. Biosynthesis, transport, regulation and chemical synthesis of natural siderophores and their analogues is of considerable interest for the protein and peptide chemist. This review gives an overview of the structural classes of peptidic siderophores, along with data on their biosynthesis. On a number of representative examples, strategies and schemes of their chemical synthesis are described.

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“…The direct incorporation of acylated L-5-hydroxy-ornithines (with acetyl for ferrichrome and methylglutaconyl for ferrichrome A) has been demonstrated by Diekmann et al [5,6] A nonribosomal peptide synthetase (NRPS) in Schizosaccharomyces pombe, which possesses an unusual structure incorporating three adenylation domains, six thiolation domains and six condensation domains, has been shown to produce the cyclohexapeptide siderophore ferrichrome. One of the adenylation domains is truncated and contains a distorted key motif.…”

Section: Introductionmentioning

confidence: 95%

Nonribosomal Peptide Synthesis in Schizosaccharomyces pombe and the Architectures of Ferrichrome‐Type Siderophore Synthetases in Fungi

et al. 2006

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A nonribosomal peptide synthetase (NRPS) in Schizosaccharomyces pombe, which possesses an unusual structure incorporating three adenylation domains, six thiolation domains and six condensation domains, has been shown to produce the cyclohexapeptide siderophore ferrichrome. One of the adenylation domains is truncated and contains a distorted key motif. Substrate-binding specificities of the remaining two domains were assigned by molecular modelling to glycine and to N-acetyl-N-hydroxy-L-ornithine. Hexapeptide siderophore synthetase genes of Magnaporthe grisea and Fusarium graminearum were both identified and analyzed with respect to substrate-binding sites, and the predicted product ferricrocin was identified in each. A comparative analysis of these synthetase systems, including those of the basidiomycete Ustilago maydis, the homobasidiomycete Omphalotus olearius and the ascomycetes Aspergillus nidulans, Aspergillus fumigatus, Fusarium graminearum, Cochliobolus heterostrophus, Neurospora crassa and Aureobasidium pullulans, revealed divergent domain compositions with respect to their number and positioning, although all produce similar products by iterative processes. A phylogenetic analysis of both NRPSs and associated L-N5-ornithine monooxygenases revealed that ferrichrome-type siderophore biosynthesis has coevolved in fungi with varying in trans interactions of NRPS domains.

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Biosynthesis of sideramines in fungi. Fusigen synthetase from extracts of Fusarium cubense

Cited by 19 publications

References 14 publications

Characterization of theUstilago maydis sid2Gene, Encoding a Multidomain Peptide Synthetase in the Ferrichrome Biosynthetic Gene Cluster

Characterization of theUstilago maydis sid2Gene, Encoding a Multidomain Peptide Synthetase in the Ferrichrome Biosynthetic Gene Cluster

Peptide siderophores

Nonribosomal Peptide Synthesis in Schizosaccharomyces pombe and the Architectures of Ferrichrome‐Type Siderophore Synthetases in Fungi

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