coprogen has been researched along with ferricrocin* in 5 studies
5 other study(ies) available for coprogen and ferricrocin
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Linear fusigen as the major hydroxamate siderophore of the ectomycorrhizal Basidiomycota Laccaria laccata and Laccaria bicolor.
A screening for siderophores produced by the ectomycorrhizal fungi Laccaria laccata and Laccaria bicolor in synthetic low iron medium revealed the release of several different hydroxamate siderophores of which four major siderophores could be identified by high resolution mass spectrometry. While ferricrocin, coprogen and triacetylfusarinine C were assigned as well as other known fungal siderophores, a major peak of the siderophore mixture revealed an average molecular mass of 797 for the iron-loaded compound. High resolution mass spectrometry indicated an absolute mass of m/z = 798.30973 ([M + H](+)). With a relative error of Δ = 0.56 ppm this corresponds to linear fusigen (C33H52N6O13Fe; MW = 797.3). The production of large amounts of linear fusigen by these basidiomycetous mycorrhizal fungi may possibly explain the observed suppression of plant pathogenic Fusarium species. For comparative purposes Fusarium roseum was included in this study as a well known producer of cyclic and linear fusigen. Topics: Antibiosis; Chromatography, High Pressure Liquid; Culture Media; Ferric Compounds; Ferrichrome; Fusarium; Hydroxamic Acids; Iron; Laccaria; Mass Spectrometry; Molecular Weight; Plant Roots; Siderophores; Tracheophyta | 2013 |
Structural requirements for the activity of the MirB ferrisiderophore transporter of Aspergillus fumigatus.
Siderophores have been identified as virulence factors in the opportunistic fungal pathogen Aspergillus fumigatus. The 14-pass transmembrane protein MirB is postulated to function as a siderophore transporter, responsible for uptake of the hydroxamate siderophore N,N',N″-triacetylfusarinine C (TAFC). Our aim was to identify amino acids of A. fumigatus MirB that are crucial for uptake of TAFC. Site-directed mutagenesis was used to create MirB mutants. Expression of wild-type and mutant proteins in the Saccharomyces cerevisiae strain PHY14, which lacks endogenous siderophore transporters, was confirmed by Western blotting. TAFC transport assays using (55)Fe-labeled TAFC and growth assays with Fe-TAFC as the sole iron source identified alanine 125, tyrosine 577, loop 3, and the second half of loop 7 (Loop7Del2) as crucial for function, since their substitution or deletion abrogated uptake completely. Wild-type MirB transported ferricrocin and coprogen as well as TAFC but not ferrichrysin. MirB was localized by fluorescence microscopy using antisera raised against a MirB extracellular loop peptide. Immunofluorescence microscopy showed that in yeast, wild-type MirB had a punctate distribution under the plasma membrane, as did the A125D and Y577A strains, indicating that the defect in transport of these mutants was unlikely to be due to mislocalization or degradation. MirB immunolocalization in A. fumigatus showed that the transporter was found in vesicles which cycled between the cytoplasm and the plasma membrane and was concentrated at the hyphal tips. The location of MirB was not influenced by the presence of the siderophore TAFC but was sensitive to internal iron stores. Topics: Amino Acids; Aspergillus fumigatus; Biological Transport; Blotting, Western; Cell Membrane; Computational Biology; Cytoplasm; Ferric Compounds; Ferrichrome; Fungal Proteins; Hydroxamic Acids; Hyphae; Iron; Membrane Transport Proteins; Microscopy, Fluorescence; Mutagenesis, Site-Directed; Proteolysis; Saccharomyces cerevisiae; Siderophores | 2012 |
Ferricrocin functions as the main intracellular iron-storage compound in mycelia of Neurospora crassa.
Neurospora crassa produces several structurally distinct siderophores: coprogen, ferricrocin, ferrichrome C and some minor unknown compounds. Under conditions of iron starvation, desferricoprogen is the major extracellular siderophore whereas desferriferricrocin and desferriferichrome C are predominantly found intracellularly. Mössbauer spectroscopic analyses revealed that coprogen-bound iron is rapidly released after uptake in mycelia of the wild-type N. crassa 74A. The major intracellular target of iron distribution is desferriferricrocin. No ferritin-like iron pools could be detected. Ferricrocin functions as the main intracellular iron-storage peptide in mycelia of N. crassa. After uptake of ferricrocin in both the wild-type N. crassa 74A and the siderophore-free mutant N. crassa arg-5 ota aga, surprisingly little metabolization (11%) could be observed. Since ferricrocin is the main iron-storage compound in spores of N. crassa, we suggest that ferricrocin is stored in mycelia for inclusion into conidiospores. Topics: Biological Transport, Active; Ferrichrome; Hydroxamic Acids; Iron; Iron Chelating Agents; Mutation; Neurospora crassa; Siderophores; Spectroscopy, Mossbauer; Spores, Fungal | 1988 |
Inhibitory effect of the partially resolved coordination isomers of chromic desferricoprogen on coprogen uptake in Neurospora crassa.
Two partially resolved chromatographic fractions of geometrical and optical isomers of the chromic complexes of desferricoprogen, a siderophore from Neurospora crassa, were obtained from high-pressure liquid chromatography on a reverse-phase matrix. The first fraction was identified as a cis complex with a 20% diastereomeric excess of the lambda isomer. The second fraction was identified as a mixture of several of the possible trans isomers with a net 20% diastereomeric excess of the delta isomers. These fractions were used to evaluate the stereospecificity of the coprogen-mediated iron uptake system with respect to the metal coordination center. Fraction II competitively inhibited coprogen uptake, whereas fraction I showed only slight inhibition. N. crassa accumulated chromium from fraction II faster than the rate of chromium uptake from fraction I. Neither fraction had a significant effect on the uptake of ferricrocin, suggesting that coprogen and ferricrocin are taken up by different receptor systems. Topics: Chromium; Circular Dichroism; Diketopiperazines; Ferrichrome; Hydroxamic Acids; Iron Chelating Agents; Iron Radioisotopes; Neurospora; Neurospora crassa; Stereoisomerism | 1986 |
Cellular and extracellular siderophores of Aspergillus nidulans and Penicillium chrysogenum.
Aspergillus nidulans and Penicillium chrysogenum produce specific cellular siderophores in addition to the well-known siderophores of the culture medium. Since this was found previously in Neurospora crassa, it is probably generally true for filamentous ascomycetes. The cellular siderophore of A. nidulans is ferricrocin; that of P. chrysogenum is ferrichrome. A. nidulans also contains triacetylfusigen, a siderophore without apparent biological activity. Conidia of both species lose siderophores at high salt concentrations and become siderophore dependent. This has also been found in N. crassa, where lowering of the water activity has been shown to be the causal factor. We used an assay procedure based on this dependency to reexamine the extracellular siderophores of these species. During rapid mycelial growth, both A. nidulans and P. chrysogenum produced two highly active, unidentified siderophores which were later replaced by a less active or inactive product--coprogen in the case of P. chrysogenum and triacetylfusigen in the case of A. nidulans. N. crassa secreted coprogen only. Fungal siderophore metabolism is varied and complex. Topics: Aspergillus nidulans; Chemical Phenomena; Chemistry; Ferrichrome; Hydroxamic Acids; Iron Chelating Agents; Neurospora crassa; Penicillium; Penicillium chrysogenum; Siderophores | 1981 |