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Related Experiment Videos

Cytoplasmic chaperonin containing TCP-1: structural and functional characterization

R Melki1, G Batelier, S Soulié

  • 1Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France. melki@lebs.cnrs-gif.fr

Biochemistry
|May 13, 1997
PubMed
Summary

The cytoplasmic chaperonin containing TCP-1 (CCT) binds unfolded proteins with high affinity. Nucleotide binding regulates CCT

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Area of Science:

  • Molecular biology
  • Protein folding
  • Cellular machinery

Background:

  • Cytoplasmic chaperonin containing TCP-1 (CCT/TRiC) is essential for folding actin and tubulin.
  • Nucleotide exchange and ATP hydrolysis modulate CCT's substrate interaction affinity.

Purpose of the Study:

  • To investigate CCT's conformational changes and substrate binding.
  • To elucidate the role of nucleotides in CCT function.

Main Methods:

  • Binding assays with labeled denatured proteins and cell extracts.
  • Electron microscopy, sedimentation velocity, and fluorescence spectroscopy.
  • Utilizing beta-actin and beta-tubulin as model substrates.

Main Results:

  • CCT exhibits high-affinity binding to diverse unfolded proteins in the absence of nucleotides.

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  • The CCT complex can simultaneously accommodate two substrate protein chains.
  • Distinct conformational states of CCT were observed in ATP- and ADP-bound forms, and upon substrate binding.

    • Conclusions:

    • CCT's nucleotide-dependent conformational changes are crucial for substrate binding regulation.
    • A model for substrate association and nucleotide-mediated affinity control by CCT was proposed.