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.

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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