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Atomic force microscopy detects changes in the interaction forces between GroEL and substrate proteins

A Vinckier1, P Gervasoni, F Zaugg

  • 1Department of Biochemistry, Swiss Federal Institute of Technology, ETH Zentrum, Zürich. vinckier@anatomie.unizh.ch

Biophysical Journal
|June 23, 1998
PubMed
Summary
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Atomic force microscopy revealed Escherichia coli chaperonin GroEL's structure and function. ATP binding induces GroEL conformational changes, affecting substrate protein interactions and binding forces.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • The Escherichia coli chaperonin GroEL is a crucial protein complex involved in protein folding.
  • Understanding GroEL's structural dynamics and substrate interactions is key to deciphering its molecular mechanism.

Purpose of the Study:

  • To investigate the structure of Escherichia coli chaperonin GroEL using tapping-mode atomic force microscopy (AFM).
  • To study the interaction forces between GroEL and substrate proteins under various conditions using force spectroscopy.
  • To detect GroEL conformational changes upon nucleotide binding.

Main Methods:

  • Tapping-mode atomic force microscopy (AFM) for high-resolution imaging of GroEL structure in liquid.
  • Force spectroscopy to measure interaction forces between GroEL and substrate proteins (citrate synthase and RTEM beta-lactamase).

Related Experiment Videos

  • Controlled experimental conditions including the presence of ATP and ATPgammaS.

    • Main Results:

    • High-resolution AFM images showed GroEL adsorbed on mica with its substrate-binding site accessible.
    • Interaction forces between GroEL and substrate proteins decreased in the presence of ATP, but not ATPgammaS.
    • Interaction forces were lower for native-like proteins compared to fully denatured proteins.
    • Interaction energy with GroEL increased with increasing molecular weight of the substrate protein.
    • Specific GroEL conformational changes were detected upon nucleotide binding.

    Conclusions:

    • AFM provides detailed structural insights into GroEL orientation and accessibility of its binding sites.
    • ATP binding is critical for inducing GroEL conformational changes that modulate substrate interactions.
    • The study elucidates the role of ATP in GroEL's chaperone activity and substrate binding dynamics.