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- W2433258312 abstract "Functions of proteins critically rely on their conformation, but understanding conformational transitions in membrane proteins poses challenges because of their hydrophobic and aggregation-prone nature. In the current study, we focus on the two topologically unique intramembrane rhomboid proteases: HiGlpG and PsAarA, with an aim to understand the relationship between the extent of unfolding upon exposure to a chemical denaturant or temperature, and regain of native activity in the reassembled form. Whereas thermal denaturation has irreversible destabilizing effects on both proteins, unfolding induced by guanidinium chloride is completely reversible for HiGlpG but only partly reversible for PsAarA. For both rhomboid proteases, circular dichroism spectroscopy as a function of denaturant concentration reveals a broad, gradual transition from the native, folded state to the denatured, unfolded state, thus arguing against a classical two-state model as found for many globular soluble proteins. Upon removal of denaturant, protein refolding and dimer re-association result in regain of native-like activity, as confirmed by fluorescence-based enzyme kinetics. This concerted biophysical and functional analysis demonstrates that the simple 6TM organization of HiGlpG is more robust than the 6+1TM organization of PsAarA." @default.
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- W2433258312 date "2016-02-01" @default.
- W2433258312 modified "2023-10-14" @default.
- W2433258312 title "Understanding Structural and Functional Stability of two Rhomboid Proteases: HiGlpG and PsAarA" @default.
- W2433258312 doi "https://doi.org/10.1016/j.bpj.2015.11.1268" @default.
- W2433258312 hasPublicationYear "2016" @default.
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