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The four aldehyde oxidases of Drosophila melanogaster have different gene expression patterns and enzyme substrate specificities

  • In the genome of Drosophila melanogaster, four genes coding for aldehyde oxidases (AOX1-4) were identified on chromosome 3. Phylogenetic analysis showed that the AOX gene cluster evolved via independent duplication events in the vertebrate and invertebrate lineages. The functional role and the substrate specificity of the distinct Drosophila AOX enzymes is unknown. Two loss-of-function mutant alleles in this gene region, low pyridoxal oxidase (Po-lpo) and aldehyde oxidase-1 (Aldox-1(n1)) are associated with a phenotype characterized by undetectable AOX enzymatic activity. However, the genes involved and the corresponding mutations have not yet been identified. In this study we characterized the activities, substrate specificities and expression profiles of the four AOX enzymes in D. melanogaster. We show that the Po-lpo-associated phenotype is the consequence of a structural alteration of the AOX1 gene. We identified an 11-bp deletion in the Po-lpo allele, resulting in a frame-shift event, which removes the molybdenum cofactor domainIn the genome of Drosophila melanogaster, four genes coding for aldehyde oxidases (AOX1-4) were identified on chromosome 3. Phylogenetic analysis showed that the AOX gene cluster evolved via independent duplication events in the vertebrate and invertebrate lineages. The functional role and the substrate specificity of the distinct Drosophila AOX enzymes is unknown. Two loss-of-function mutant alleles in this gene region, low pyridoxal oxidase (Po-lpo) and aldehyde oxidase-1 (Aldox-1(n1)) are associated with a phenotype characterized by undetectable AOX enzymatic activity. However, the genes involved and the corresponding mutations have not yet been identified. In this study we characterized the activities, substrate specificities and expression profiles of the four AOX enzymes in D. melanogaster. We show that the Po-lpo-associated phenotype is the consequence of a structural alteration of the AOX1 gene. We identified an 11-bp deletion in the Po-lpo allele, resulting in a frame-shift event, which removes the molybdenum cofactor domain of the encoded enzyme. Furthermore, we show that AOX2 activity is detectable only during metamorphosis and characterize a Minos-AOX2 insertion in this developmental gene that disrupts its activity. We demonstrate that the Aldox-1(n1) phenotype maps to the AOX3 gene and AOX4 activity is not detectable in our assays.show moreshow less

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Metadaten
Author details:Zvonimir Marelja, Miriam Dambowsky, Marco Bolis, Marina L. Georgiou, Enrico Garattini, Fanis Missirlis, Silke LeimkühlerORCiDGND
DOI:https://doi.org/10.1242/jeb.102129
ISSN:0022-0949
ISSN:1477-9145
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/24737760
Title of parent work (English):The journal of experimental biology
Publisher:Company of Biologists Limited
Place of publishing:Cambridge
Publication type:Article
Language:English
Year of first publication:2014
Publication year:2014
Release date:2017/03/27
Tag:Aldehyde oxidase; Drosophila melanogaster; Gene duplication; Molybdoenzymes; Substrate specificities
Volume:217
Issue:12
Number of pages:11
First page:2201
Last Page:2211
Funding institution:Deutsche Forschungsgemeinschaft (DFG) [LE1171/8-1]; Consejo Nacional de Ciencia y Tecnologia project [179835]; European Molecular Biology Organisation (EMBO) [ASTF 226-2011]; Studienstiftung des deutschen Volkes; National Institutes of Health [OD010949-10]
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer review:Referiert
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