FEBS Letters · 1994 · 75 citations · 34 references
Life SciencesBiochemistryMolecular BiologyEnzymologyMitochondrial BiologyProtein FoldingChaperone-assisted FoldingChaperone-mediated FoldingEnzyme StabilityMolecular ChaperonesProtein Folding PathwaysProtein Folding ThermodynamicsAtp-dependent Folding MechanismsChaperone-mediated Folding PathwaysChaperone-substrate InteractionsChaperonin FunctionChaperonin-mediated FoldingCytosolic ChaperonesNative State AssemblyNative-state Stability
mMDH and cMDH are structurally homologous enzymes which show very different responses to chaperonins during folding. The hydrophilic and stable cMDH is bound by cpn60 but released by Mg-ATP alone, while the hydrophobic and unstable mMDH requires both Mg-ATP and cpn10. Citrate equalises the stability of the native state of the two proteins but has no effect on the co-chaperonin requirement, implying that hydrophobicity, and not stability, is the determining factor. The yield and rate of folding of cMDH is unaffected while that of mMDH is markedly increased by the presence of cpn60, cpn10 and Mg-ATP. In 200 mM orthophosphate, chaperonins do not enhance the rate of folding of mMDH, but in low phosphate concentrations chaperonin-assisted folding is 3-4-times faster.
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GroE facilitates refolding of citrate synthase by suppressing aggregation
Johannes Büchner, Marion Schmidt, Miriam Fuchs et al. · Biochemistry · 1991 · 487 citations