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Related Experiment Videos

DnaJ potentiates the interaction between DnaK and alpha-helical peptides

A de Crouy-Chanel1, R S Hodges, M Kohiyama

  • 1Institut Jacques Monod, Université Paris 7, France.

Biochemical and Biophysical Research Communications
|April 28, 1997
PubMed
Summary

Molecular chaperones like E. coli DnaK bind unfolded proteins. Co-chaperone DnaJ enhances DnaK

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Area of Science:

  • Molecular biology
  • Protein biochemistry

Background:

  • Molecular chaperones assist protein folding, targeting, and renaturation.
  • E. coli DnaK preferentially binds positively charged, hydrophobic peptides in extended conformations.

Purpose of the Study:

  • To investigate the interaction of the DnaK chaperone with alpha-helical peptides.
  • To determine the role of co-chaperone DnaJ in modulating this interaction.

Main Methods:

  • Peptide binding assays were used to assess the affinity of DnaK for alpha-helical peptides.
  • Experiments were conducted in the presence and absence of ATP and the co-chaperone DnaJ.

Main Results:

  • DnaK exhibited low affinity for alpha-helical peptides in isolation.

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  • The presence of DnaJ and ATP significantly enhanced DnaK's interaction with alpha-helical peptides.
  • This enhancement suggests DnaJ induces a conformational change in DnaK.

    • Conclusions:

    • The DnaK/DnaJ/GrpE chaperone system effectively interacts with alpha-helical peptides, a common protein secondary structure.
    • This interaction is crucial for the chaperone machine's role in protein folding and stress-induced renaturation.