Nonribosomal Peptide Synthesis in Schizosaccharomyces pombe and the Architectures of Ferrichrome-Type Siderophore Synthetases in Fungi
Autor: | Ralf Dieckmann, Kirsten Göttling, Ines Dueñas, Hans von Döhren, Norbert F. Käufer, Pawel Durek, Eike Staub, Torsten Neuhof, Torsten Schwecke, Susanne Zock-Emmenthal |
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Rok vydání: | 2006 |
Předmět: |
Models
Molecular Siderophore Protein Conformation Molecular Sequence Data Siderophores Cochliobolus heterostrophus Sensitivity and Specificity Biochemistry Catalysis Neurospora crassa Aspergillus fumigatus chemistry.chemical_compound Nonribosomal peptide Aspergillus nidulans Schizosaccharomyces Amino Acid Sequence Peptide Synthases Molecular Biology Chromatography High Pressure Liquid Phylogeny Ferrichrome chemistry.chemical_classification Binding Sites Molecular Structure biology Organic Chemistry Fungi food and beverages biology.organism_classification chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Schizosaccharomyces pombe Peptide Biosynthesis Nucleic Acid-Independent Molecular Medicine |
Zdroj: | ChemBioChem. 7:612-622 |
ISSN: | 1439-4227 |
Popis: | 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. |
Databáze: | OpenAIRE |
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