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Related Experiment Videos

Chaperone activity of DsbC.

J Chen1, J L Song, S Zhang

  • 1National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, China.

The Journal of Biological Chemistry
|July 3, 1999
PubMed
Summary

DsbC, a bacterial disulfide isomerase, exhibits lower enzymatic activity but stronger chaperone function than eukaryotic PDI. It aids protein refolding and prevents aggregation, with distinct substrate recognition.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • DsbC is a periplasmic disulfide isomerase in Gram-negative bacteria.
  • Eukaryotic protein disulfide isomerase (PDI) is a well-studied enzyme with similar functions.
  • Comparing DsbC and PDI offers insights into conserved and divergent protein folding mechanisms.

Purpose of the Study:

  • To compare the enzymatic and chaperone activities of bacterial DsbC with eukaryotic PDI.
  • To investigate the role of specific residues (e.g., Cys98) in DsbC function.
  • To explore the substrate specificity and interaction of DsbC and PDI with folding intermediates.

Main Methods:

  • In vitro refolding assays using denatured D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and lysozyme.

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  • Enzymatic activity assays for isomerase and thiol-protein oxidoreductase functions.
  • Chemical modification (carboxymethylation) of DsbC to assess the role of Cys98.
  • Inhibition studies using various peptides and modified proteins.

    • Main Results:

    • DsbC showed approximately 30% of PDI's isomerase and oxidoreductase activity but superior chaperone activity in GAPDH refolding and aggregation suppression.
    • Carboxymethylation of DsbC at Cys98 reduced enzyme activity but only partially affected chaperone function.
    • DsbC and PDI exhibited additive effects on GAPDH reactivation when used together.
    • DsbC's activity was inhibited by larger RNase substrates, unlike PDI, which was also inhibited by smaller peptides.

    Conclusions:

    • DsbC possesses significant chaperone activity, potentially exceeding that of PDI under certain conditions.
    • DsbC and PDI may recognize different folding intermediates, contributing to their distinct functional profiles.
    • The study highlights the dual role of DsbC as both a disulfide isomerase and a chaperone.