Pathway of Glycine Betaine Biosynthesis in Aspergillus fumigatus

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Titel: Pathway of Glycine Betaine Biosynthesis in Aspergillus fumigatus
Autoren: Lambou, Karine, Pennati, Andrea, Valsecchi, Isabel, Tada, Rui, Sherman, Stephen, Sato, Hajime, Beau, Remi, Gadda, Giovanni, Latgé, Jean-Paul
Weitere Verfasser: Aspergillus, Institut Pasteur Paris (IP), Georgia State University, University System of Georgia (USG), Bruker Biospin KK Japan, This study was supported in part by NSF-CAREER grant MCB-0545712 and NSF grant MCB-1121695 (G.G.) and European grants ALLFUNFP7260338 and ESF Fuminomics RNP 06-132 (J.-P.L.)., European Project: 260338,FP7-HEALTH-2010-single-stage,FP7-HEALTH-2010-single-stage,ALLFUN(2010)
Quelle: ISSN: 1535-9778.
Verlagsinformationen: CCSD
American Society for Microbiology
Publikationsjahr: 2013
Bestand: Institut Pasteur: HAL
Schlagwörter: MESH: Alcohol Oxidoreductases/genetics, MESH: Alcohol Oxidoreductases/metabolism, MESH: Flavin-Adenine Dinucleotide/metabolism, MESH: Fungal Proteins/genetics, MESH: Fungal Proteins/metabolism, MESH: Gene Expression Regulation, Fungal, MESH: Kinetics, MESH: Mutation, MESH: Mycelium/genetics, MESH: Mycelium/metabolism, MESH: Species Specificity, MESH: Spores, Fungal/genetics, MESH: Aspergillus fumigatus/genetics, Fungal/metabolism, MESH: Aspergillus fumigatus/metabolism, MESH: Betaine/analogs & derivatives, MESH: Betaine/metabolism, MESH: Betaine-Aldehyde Dehydrogenase/genetics, MESH: Betaine-Aldehyde Dehydrogenase/metabolism, MESH: Choline/metabolism, MESH: Enzyme Assays, [SDV]Life Sciences [q-bio], [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, [SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology
Beschreibung: International audience ; The choline oxidase (CHOA) and betaine aldehyde dehydrogenase (BADH) genes identified in Aspergillus fumigatus are present as a cluster specific for fungal genomes. Biochemical and molecular analyses of this cluster showed that it has very specific biochemical and functional features that make it unique and different from its plant and bacterial homologs. A. fumigatus ChoAp catalyzed the oxidation of choline to glycine betaine with betaine aldehyde as an intermediate and reduced molecular oxygen to hydrogen peroxide using FAD as a cofactor. A. fumigatus Badhp oxidized betaine aldehyde to glycine betaine with reduction of NAD(+) to NADH. Analysis of the AfchoAΔ::HPH and AfbadAΔ::HPH single mutants and the AfchoAΔAfbadAΔ::HPH double mutant showed that AfChoAp is essential for the use of choline as the sole nitrogen, carbon, or carbon and nitrogen source during the germination process. AfChoAp and AfBadAp were localized in the cytosol of germinating conidia and mycelia but were absent from resting conidia. Characterization of the mutant phenotypes showed that glycine betaine in A. fumigatus functions exclusively as a metabolic intermediate in the catabolism of choline and not as a stress protectant. This study in A. fumigatus is the first molecular, cellular, and biochemical characterization of the glycine betaine biosynthetic pathway in the fungal kingdom.
Publikationsart: article in journal/newspaper
Sprache: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/23563483; info:eu-repo/grantAgreement//260338/EU/Fungi in the setting of inflammation, allergy and autoimmune diseases:Translating basic science into clinical practices/ALLFUN; PUBMED: 23563483; PUBMEDCENTRAL: PMC3675988
DOI: 10.1128/EC.00348-12
Verfügbarkeit: https://hal.science/hal-02468278
https://doi.org/10.1128/EC.00348-12
Dokumentencode: edsbas.7EBA5DA6
Datenbank: BASE
Beschreibung
Abstract:International audience ; The choline oxidase (CHOA) and betaine aldehyde dehydrogenase (BADH) genes identified in Aspergillus fumigatus are present as a cluster specific for fungal genomes. Biochemical and molecular analyses of this cluster showed that it has very specific biochemical and functional features that make it unique and different from its plant and bacterial homologs. A. fumigatus ChoAp catalyzed the oxidation of choline to glycine betaine with betaine aldehyde as an intermediate and reduced molecular oxygen to hydrogen peroxide using FAD as a cofactor. A. fumigatus Badhp oxidized betaine aldehyde to glycine betaine with reduction of NAD(+) to NADH. Analysis of the AfchoAΔ::HPH and AfbadAΔ::HPH single mutants and the AfchoAΔAfbadAΔ::HPH double mutant showed that AfChoAp is essential for the use of choline as the sole nitrogen, carbon, or carbon and nitrogen source during the germination process. AfChoAp and AfBadAp were localized in the cytosol of germinating conidia and mycelia but were absent from resting conidia. Characterization of the mutant phenotypes showed that glycine betaine in A. fumigatus functions exclusively as a metabolic intermediate in the catabolism of choline and not as a stress protectant. This study in A. fumigatus is the first molecular, cellular, and biochemical characterization of the glycine betaine biosynthetic pathway in the fungal kingdom.
DOI:10.1128/EC.00348-12