Ferricrocin functions as the main intracellular iron-storage compound in mycelia ofNeurospora crassa

Matzanke, Berthold F.; Bill, E.; Trautwein, Alfred X.; Winkelmann, G.

doi:10.1007/bf01128013

Cited by 38 publications

(19 citation statements)

References 14 publications

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“…The corresponding domains found in the synthetases of N. crassa, F. graminearum and A. pullulans are likely also to accept Ala. This finding is substantiated by the production of ferrichrome C in N. crassa containing the sequence Gly-Ser-Gly and Gly-Ala-Gly, [24] which we have also detected in M. grisea and F. graminearum.…”

Section: Assignment Of Substrate-binding Sites-the Code Of Nonribosomsupporting

confidence: 69%

“…While ferricrocin production was known for N. crassa, [24] we have now also shown the formation of this siderophore in M. grisea and G. zeae under iron limitation conditions. Pocket geometries identical to those in S. pombe were detected in the first adenylation domains of all four ascomycetes.…”

Section: Assignment Of Substrate-binding Sites-the Code Of Nonribosommentioning

confidence: 91%

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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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Section: Assignment Of Substrate-binding Sites-the Code Of Nonribosomsupporting

confidence: 69%

Section: Assignment Of Substrate-binding Sites-the Code Of Nonribosommentioning

confidence: 91%

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

et al. 2006

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“…In Neurospora crassa intracellular ferricrocin functions as iron-storage compound and is translocated to the conidia (Matzanke et al, 1988). The production of this siderophore was increased in the presence of iron.…”

Section: Magnaporthe Grisea Produces Siderophores Of the Hydroxamate mentioning

confidence: 99%

Siderophores Produced by Magnaporthe grisea in the Presence and Absence of Iron

Antelo

Hof

Welzel

et al. 2006

Zeitschrift Für Naturforschung C

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An analysis of siderophores produced by Magnaporthe grisea revealed the presence of one intracellular storage siderophore, ferricrocin, and four coprogen derivatives secreted into the medium under iron depletion. Structural analysis showed that the compounds are coprogen, coprogen B, 2-N-methylcoprogen and 2-Nmethylcoprogen B. Siderophore production under low and high iron conditions was quantified.

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“…(i) FC accumulation increases under conditions of intracellular iron excess (4,9,14); (ii) FC deficiency reduces the iron content of conidia by 34% and 76% in A. nidulans and A. fumigatus, respectively (4, 13); (iii) FC deficiency reduces conidial germination efficiency (4, 13); and (iv) FC deficiency concomitantly increases the labile iron pool and decreases the oxidative stress resistance of hyphae (3,13). Similarly, FC was found to be involved in hyphal and conidial iron storage in Neurospora crassa (8).…”

mentioning

confidence: 99%

Ferricrocin, a Siderophore Involved in Intra- and Transcellular Iron Distribution in Aspergillus fumigatus

Wallner¹,

Blatzer²,

Schrettl³

et al. 2009

Appl Environ Microbiol

115

102

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Iron is an essential metal for virtually all organisms. Iron acquisition is well characterized for various organisms, whereas intracellular iron distribution is poorly understood. In contrast to bacteria, plants, and animals, most fungi lack ferritin-mediated iron storage but possess an intracellular siderophore shown to be involved in iron storage. Here we demonstrate that deficiency in the intracellular siderophore ferricrocin causes iron starvation in conidia of Aspergillus fumigatus, demonstrating that ferricrocin is also involved in intra-and transcellular iron distribution. Thus, ferricrocin represents the first intracellular iron transporter identified in any organism.Virtually all organisms require iron as an indispensable cofactor for various metabolic processes, including electron transport and redox reactions. Excess or incorrect storage of iron, however, is toxic, as this metal has the capacity to reinforce the production of reactive oxygen species. Therefore, organisms have evolved precisely regulated iron acquisition systems, which are well characterized in numerous prokaryotes and eukaryotes. In contrast, mechanisms for intracellular distribution of acquired iron are poorly understood. We investigated these mechanisms in Aspergillus fumigatus, a typical saprophytic ascomycete, which has become the most common airborne fungal pathogen of humans, causing life-threatening invasive disease especially in immunocompromised patients (16). A. fumigatus employs four siderophores (low-molecularmass ferric iron chelators) for maintenance of iron homeostasis (5): it excretes two siderophores for solubilization and uptake of iron, and it accumulates two structurally different siderophores, ferricrocin (FC) and its hydroxylated derivative hydroxy-FC, within hyphae and conidia, respectively. Both intracellular siderophores are believed to be involved in intracellular iron storage. The siderophore system became a matter of particular interest as it represents an attractive target for antifungal therapy due to its requirement for virulence of A. fumigatus and its lack in mammalian hosts (12, 13). Recently, extra-and intracellular siderophores have also been implicated in the phytopathogenicity of various ascomycetes (6, 11). Here we demonstrate that intracellular siderophores are also involved in the intracellular long-distance distribution of iron.Extracellular siderophores are utilized by most fungi and bacteria and some plants, whereas intracellular siderophores are found exclusively in fungi, which in contrast to bacteria, plants, and animals lack ferritin-mediated iron storage (5). The function of intracellular siderophores has been studied in the most detail with Aspergillus nidulans and A. fumigatus (5). Several lines of evidence support a role for FC and hydroxy-FC in iron storage in these fungi. (i) FC accumulation increases under conditions of intracellular iron excess (4, 9, 14); (ii) FC deficiency reduces the iron content of conidia by 34% and 76% in A. nidulans and A. fumigatus, respectively (4, 13); ...

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Ferricrocin functions as the main intracellular iron-storage compound in mycelia ofNeurospora crassa

Cited by 38 publications

References 14 publications

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

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

Siderophores Produced by Magnaporthe grisea in the Presence and Absence of Iron

Ferricrocin, a Siderophore Involved in Intra- and Transcellular Iron Distribution in Aspergillus fumigatus

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