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Related Experiment Videos

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

N A Ranson1, S G Burston, A R Clarke

  • 1Molecular Recognition Centre, School of Medical Sciences, University of Bristol, UK.

Journal of Molecular Biology
|March 7, 1997
PubMed
Summary
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The molecular chaperones GroEL-GroES and ATP accelerate mitochondrial malate dehydrogenase (mMDH) folding. Folding occurs within the chaperonin complex, with ATP driving a cycle of substrate binding, encapsulation, and release.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • Mitochondrial malate dehydrogenase (mMDH) requires assistance for rapid folding.
  • Molecular chaperones like GroEL-GroES are crucial for protein folding in vivo.

Purpose of the Study:

  • To investigate the mechanism by which GroEL-GroES and ATP facilitate mMDH folding.
  • To determine the kinetics and stoichiometry of mMDH-chaperonin interaction.

Main Methods:

  • Enzyme kinetics assays to measure mMDH folding rates.
  • Chaperonin binding and trapping experiments.
  • Stoichiometry and dissociation constant determination.

Main Results:

  • GroEL-GroES and ATP significantly increase mMDH folding rates.

Related Experiment Videos

  • Optimal folding occurs at equimolar stoichiometry of mMDH subunits to GroEL oligomers.
  • mMDH folding occurs within the chaperonin complex with minimal inhibition.
  • Substrate dwell time on the chaperonin is brief (20 seconds), correlating with ATP turnover.

    • Conclusions:

    • ATP drives the GroEL-GroES complex through acceptor, encapsulation, and ejector states.
    • Folding proceeds efficiently within the encapsulated state, independent of GroEL surface interactions.
    • The chaperonin cycle facilitates rapid folding and release of mMDH.