Abstract
Here, we report the identification and characterization of the first proton channels from fungi. The fungal proteins are related to animal voltage-gated Hv channels and are conserved in both higher and lower fungi. Channels from Basidiomycota and Ascomycota appear to be evolutionally and functionally distinct. Representatives from the two phyla share several features with their animal counterparts, including structural organization and strong proton selectivity, but they differ from each other and from animal Hvs in terms of voltage range of activation, pharmacology, and pH sensitivity. The activation gate of Hv channels is believed to be contained within the transmembrane core of the protein and little is known about contributions of peripheral regions to the activation mechanism. Using a chimeragenesis approach, we find that intra- and extracellular peripheral regions are main determinants of the voltage range of activation in fungal channels, highlighting the role of these overlooked components in channel gating.
Highlights
We report the identification and characterization of the first proton channels from fungi
The Hv1 channel contributes to pH homeostasis in various cell types and has important functions in the immune, respiratory, and reproductive systems[11], e.g., its activity is known to modulate the production of reactive oxygen species (ROS) by NADPH oxidase (NOX) enzymes[12,13,14]
We report the identification of members of the Hv channel family in both higher and lower fungi and the biophysical and pharmacological characterization of two of these channels: SlHv1 from Suillus luteus, a representative of the phylum Basidiomycota, and AoHv1 from Aspergillus oryzae, a representative of the phylum Ascomycota
Summary
We report the identification and characterization of the first proton channels from fungi. Protein sequence analysis (see “Methods”) indicates a similar membrane topology and structural organization for SlHv1 and AoHv1 compared to animal Hvs (Fig. 1b).
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