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Updated: Jul 24, 2026

A Rapid and Efficient Method for Assessing Pathogenicity of Ustilago maydis on Maize and Teosinte Lines
Published on: January 3, 2014
A H2O2-producing glyoxal oxidase is required for filamentous growth and pathogenicity in Ustilago maydis
B Leuthner1, C Aichinger, E Oehmen
1Bayer CropScience AG, Alfred-Nobel-Strasse 50, 40789 Monheim, Germany.
Abstract:
In the phytopathogenic fungus Ustilago maydis the mating-type loci control the transition from yeast-like to filamentous growth required for pathogenic development. In a large REMI (restriction enzyme mediated integration) screen, non-pathogenic mutants were isolated in a haploid strain that had been engineered to be pathogenic. In one of these mutants, which showed a specific morphological phenotype, the tagged gene, glo1 , was found to encode a product that is highly homologous to a glyoxal oxidase gene from the wood-rot fungus Phanerochaete chrysosporium. Glyoxal oxidase homologues are found in human, plant pathogenic fungi and in plants, but not in other mammals or yeasts. To confirm the function of the glo1 gene, null mutations were generated in compatible haploid U. maydis strains. In crosses null mutants were unable to generate filamentous dikaryons, and were completely non-pathogenic. Using a Glo1-overproducing strain we demonstrated that Glo1 is membrane bound, oxidizes a series of small aldehydes (< C4) and produces H2O2. The enzyme needs to be activated, presumably by auto-oxidation, to show full activity. A potential role for Glo1 during filamentous growth and pathogenic development of U. maydis is proposed.
Insights
The glyoxal oxidase 1 (glo1) gene is crucial for the pathogenic development of the fungus Ustilago maydis. Loss of glo1 function prevents filamentous growth and pathogenicity, highlighting its role in fungal development.
Area of Science:
- Mycology
- Plant Pathology
- Biochemistry
Background:
- The phytopathogenic fungus Ustilago maydis requires a switch from yeast-like to filamentous growth for pathogenic development, controlled by mating-type loci.
- Previous research identified non-pathogenic mutants through a restriction enzyme mediated integration (REMI) screen.
Purpose of the Study:
- To investigate the function of the glo1 gene, identified in a non-pathogenic Ustilago maydis mutant.
- To elucidate the role of glyoxal oxidase in the pathogenicity of Ustilago maydis.
Main Methods:
- Generated glo1 null mutations in Ustilago maydis.
- Performed crosses with null mutants to assess filamentous growth and pathogenicity.
- Utilized a Glo1-overproducing strain to characterize enzyme activity and localization.
Main Results:
- Glo1 is homologous to glyoxal oxidase from Phanerochaete chrysosporium and is found in various organisms but not in mammals or yeasts.
- Ustilago maydis glo1 null mutants failed to form filamentous dikaryons and were non-pathogenic.
- Glo1 is a membrane-bound enzyme that oxidizes small aldehydes (< C4) producing hydrogen peroxide (H2O2), requiring activation for full activity.
Conclusions:
- The glo1 gene product is essential for the filamentous growth and pathogenic development of Ustilago maydis.
- Glo1's enzymatic activity and requirement for activation suggest a significant role in fungal pathogenesis.
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