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Related Experiment Videos

Protein structure and import into the peroxisomal matrix.

Cécile B Brocard1, Christopher Jedeszko, Hong Chang Song

  • 1Department of Anatomy and Cell Biology, The University of Western Ontario, London, Ontario, N6A 5C1, Canada.

Traffic (Copenhagen, Denmark)
|February 1, 2003
PubMed
Summary

Proteins can be imported into peroxisomes even if unfolded. This study shows that protein tertiary structure does not affect peroxisomal import, challenging previous assumptions about protein folding and targeting.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Proteins for the peroxisomal matrix are synthesized in the cytosol and imported post-translationally.
  • Previous studies indicated that only stably folded proteins are substrates for peroxisomal import.
  • Mammalian peroxisomes lack endogenous chaperone molecules, suggesting a potential role for protein folding in import.

Purpose of the Study:

  • To investigate whether unfolded proteins are substrates for peroxisomal import.
  • To determine if protein tertiary structure influences import into peroxisomes.

Main Methods:

  • Albumin was unfolded via reduction to alter its tertiary structure, confirmed by analytical centrifugation.
  • Unfolded albumin with a PTS1 targeting signal was microinjected into cells.

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  • Peroxisomal import rates of native and unfolded albumin were compared using kinetic analysis.
  • The effect of cycloheximide on import was assessed, and co-import with hsc70 was observed.

    • Main Results:

    • Unfolded albumin molecules were successfully imported into peroxisomes.
    • Import rates for native and unfolded albumin were comparable.
    • Protein import into peroxisomes was not inhibited by cycloheximide.
    • Hsc70 chaperone molecules were observed to co-import with unfolded albumin.

    Conclusions:

    • Proteins incapable of assuming their native conformation are substrates for peroxisomal import.
    • Tertiary protein structure does not influence the import process into the peroxisomal matrix.
    • These findings support a model where protein folding is not a prerequisite for peroxisomal matrix targeting.