AoAtg26, a putative sterol glucosyltransferase, is required for autophagic degradation of peroxisomes, mitochondria, and nuclei in the filamentous fungus <i>Aspergillus oryzae</i>

Abstract

<p>Autophagy is a conserved process in eukaryotic cells for degradation of cellular proteins and organelles. In filamentous fungi, autophagic degradation of organelles such as peroxisomes, mitochondria, and nuclei occurs in basal cells after the prolonged culture, but its mechanism is not well understood. Here, we functionally analyzed the filamentous fungus <i>Aspergillus oryzae</i> AoAtg26, an ortholog of the sterol glucosyltransferase PpAtg26 involved in pexophagy in the yeast <i>Pichia pastoris</i>. Deletion of <i>Aoatg26</i> caused a severe decrease in conidiation and aerial hyphae formation, which is typically observed in the autophagy-deficient <i>A. oryzae</i> strains. In addition, cup-shaped AoAtg8-positive membrane structures were accumulated in the <i>Aoatg26</i> deletion strain, indicating that autophagic process is impaired. Indeed, the <i>Aoatg26</i> deletion strain was defective in the degradation of peroxisomes, mitochondria, and nuclei. Taken together, AoAtg26 plays an important role for autophagic degradation of organelles in <i>A. oryzae</i>, which may physiologically contribute to the differentiation in filamentous fungi.</p> <p>Involvement of AoAtg26 in autophagic organelle degradation.</p

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