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Updated: Mar 6, 2026

Toxin Induction and Protein Extraction from Fusarium spp. Cultures for Proteomic Studies
Published on: February 16, 2010
Structural reorganization of the fungal endoplasmic reticulum upon induction of mycotoxin biosynthesis
Marike Johanne Boenisch1, Karen Lisa Broz2, Samuel Owen Purvine3
1Department of Agronomy and Plant Genetics, University of Minnesota, St. Paul, MN 55108, USA.
Abstract:
Compartmentalization of metabolic pathways to particular organelles is a hallmark of eukaryotic cells. Knowledge of the development of organelles and attendant pathways under different metabolic states has been advanced by live cell imaging and organelle specific analysis. Nevertheless, relatively few studies have addressed the cellular localization of pathways for synthesis of fungal secondary metabolites, despite their importance as bioactive compounds with significance to medicine and agriculture. When triggered to produce sesquiterpene (trichothecene) mycotoxins, the endoplasmic reticulum (ER) of the phytopathogenic fungus Fusarium graminearum is reorganized both in vitro and in planta. Trichothecene biosynthetic enzymes accumulate in organized smooth ER with pronounced expansion at perinuclear- and peripheral positions. Fluorescence tagged trichothecene biosynthetic proteins co-localize with the modified ER as confirmed by co-fluorescence and co-purification with known ER proteins. We hypothesize that changes to the fungal ER represent a conserved process in specialized eukaryotic cells such as in mammalian hepatocytes and B-cells.
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