Frontiers in MicrobiologyMicrobiologyPeer-reviewed journal article
Amorphous-to-Rodlet Structural Transition Governs the Interfacial Functions of Aspergillus oryzae Hydrophobin RolA
Daiki Ida, Nao TakahashiiD, Yuki TerauchiiD, Takumi TanakaiD, Akira YoshimiiD, Hirotaka KobayashiiD, Ken MiyazawaiD, Masaya MitsuishiiD, Hiroshi YabuiD, Keietsu AbeiD
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Abstract
Hydrophobins are low-molecular-weight biosurfactant proteins that coat the cell surface of filamentous fungi, making it hydrophobic and supporting morphogenesis. On conidia, hydrophobins self-assemble to form rod-shaped multimeric structures known as rodlets. Previously, we reported that hydrophobin RolA from the industrial fungus Aspergillus oryzae first forms an amorphous film at the air-water interface and then undergoes structural rearrangement to form a densely packed rodlet film. This raised the question of whether the amorphous or the rodlet film is more important for the biological functions of RolA. In this study, to compare the properties of amorphous films with those of rodlet films, we used RolA mutants that had lost the ability to form rodlets and therefore remained in the amorphous state. We found that the rodlet film was more rigid than the amorphous film and had stronger surface activity and a greater capacity to change surface wettability. RolA altered the properties of A. oryzae conidia only when it was in the rodlet state. These findings highlight the functional versatility of RolA and show that their dynamic structural transitions directly modulate their function.
- organism: Arabidopsis
- assay: proteomics
- research focus: cell signaling & trafficking
- approach: experimental assay
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