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• W4313429512 abstract "PacC is a key transcriptional regulator of human pathogenic fungus Trichophyton rubrum with pivotal roles in pH homeostasis and virulence. We report the first biophysical characterization of the C-terminal inhibitory tail of PacC, pertinent to its physiological role in maintaining the inactive state of PacC at acidic pH which undergoes conformational changes for its proteolytic removal and activation, at alkaline pH. To gain insights into the structural features of PacC that enable the required conformational flexibility, we performed gel filtration chromatography, dynamic light scattering, circular dichroism, and 1-anilino-8-naphthalenesulfonate binding and showed that the tail exhibits properties similar to intrinsically disordered proteins, as also predicted by bioinformatics tools. We demonstrate that the C-terminal tail is conformationally flexible and attains a molten globule-like state at extremely acidic pH and undergoes biphasic GdmCl-induced unfolding in a noncooperative manner with an intermediate X state. We hypothesize that the conformational plasticity of the C-terminal tail of PacC may play a significant role in modulating its pH-dependent transcriptional activation." @default.
• W4313429512 created "2023-01-06" @default.
• W4313429512 creator A5005676982 @default.
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• W4313429512 date "2022-12-19" @default.
• W4313429512 modified "2023-09-26" @default.
• W4313429512 title "Biophysical Characterization of the C-Terminal Tail of <i>T. rubrum</i> PacC Reveals an Inherent Intrinsically Disordered Structure with pH-Induced Structural Plasticity" @default.
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• W4313429512 doi "https://doi.org/10.1021/acsomega.2c04691" @default.
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