Micelle-catalyzed domain swapping in the GlpG rhomboid protease cytoplasmic domain.

摘要: Three-dimensional domain swapping is a mode of self-interaction that can give rise to altered functional states and has been identified as the trigger event in some protein deposition diseases, yet rates interconversion between oligomeric are usually slow, with requirement for transient disruption an extensive network interactions giving large kinetic barrier. Here we demonstrate cytoplasmic Escherichia coli GlpG rhomboid protease undergoes slow dimerization via micromolar concentrations micelles be used enhance monomer-dimer exchange by more than 1000-fold. Detergents bearing phosphocholine headgroup shown true catalysts, hexadecylphosphocholine reducing 26 kcal/mol free energy barrier >11 while preserving 5 difference monomer dimer states. Catalysis involves formation micelle-bound intermediate partially unfolded structure primed swapping. Taken together, these results first catalysis swapping, using work chaperonin-like fashion unfold kinetically trapped state allow access domain-swapped form.