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Related Experiment Videos

Chaperonin function: folding by forced unfolding.

M Shtilerman1, G H Lorimer, S W Englander

  • 1The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Science (New York, N.Y.)
|April 30, 1999
PubMed
Summary
This summary is machine-generated.

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The GroEL chaperonin system partially unfolds misfolded proteins within seconds. This process, requiring ATP hydrolysis, helps proteins refold by first causing partial unfolding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • Misfolded proteins can accumulate and cause cellular dysfunction.
  • Chaperonins are molecular machines that assist protein folding.
  • The precise mechanism by which GroEL facilitates protein unfolding and refolding is not fully understood.

Purpose of the Study:

  • To investigate the ability of the GroEL chaperonin system to induce unfolding in misfolded substrate proteins.
  • To determine the kinetics and energy requirements for GroEL-mediated unfolding.
  • To elucidate the role of partial unfolding in the overall protein folding process facilitated by GroEL.

Main Methods:

  • Utilized hydrogen exchange techniques to monitor protein conformational changes.
  • Studied the GroEL chaperonin system and its substrate proteins.

Related Experiment Videos

  • Analyzed the effects of nucleoside triphosphate binding and adenosine triphosphate hydrolysis on the unfolding process.

    • Main Results:

    • GroEL-induced unfolding of the substrate protein is partial and requires the complete chaperonin system.
    • Unfolding occurs within the 13-second turnover time of the system.
    • Nucleoside triphosphate binding provides energy for single unfolding events; multiple turnovers depend on adenosine triphosphate hydrolysis.
    • Substrate protein release occurs at each turnover, irrespective of refolding status.
    • GroEL's structure appears optimized for generating mechanical force for unfolding.

    Conclusions:

    • GroEL facilitates protein folding by inducing partial unfolding in blocked, misfolded proteins.
    • The chaperonin system employs a mechanical unfolding mechanism.
    • The energy for unfolding is supplied by ATP hydrolysis, enabling iterative cycles of unfolding and release.