Metal-binding proteins and peptides in the aquatic fungi Fontanospora fusiramosa and Flagellospora curta exposed to severe metal stress

The production of thiol-containing proteins/peptides and its role in metal-binding was examined in the aquatic hyphomycetes Fontanospora fusiramosa and Flagellospora curta exposed to Cu, Cd, or Zn at concentrations inhibiting the biomass production in 80%. Heat-treated cell-free extracts were separated by size-exclusion chromatography and the thiol and metal content in the fractions was determined. F. curta, the species tolerant to metals, showed higher absolute levels of thiol compounds, which bound higher amounts of Cu and Cd than F. fusiramosa. Peptides with very low molecular weight (b9 kDa), most likely glutathione and phytochelatins, were the major Cu- and Zn-binding components in both species of aquatic hyphomycetes. In most cases, proteins with high molecular weight (N26 kDa) were induced by metal ions and they were the major Cd-binding component in both species. Proteins with characteristics of metallothioneins were also induced by exposure to metals in both species, but they showed a minor role in metal-binding, suggesting they might have other functions in fungal cells.