Publication

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Bartoszewska, M., Williams, C., Kikhney, A., Opalinski, L., van Roermund, C. W. T., de Boer, R., Veenhuis, M. & van der Klei, I. J., 10-Aug-2012, In : The Journal of Biological Chemistry. 287, 33, p. 27380-27395 16 p.

Research output: Contribution to journalArticleAcademicpeer-review

Copy link to clipboard

Documents

DOI

Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln). We show that Pln is a heptameric protein and acts as an ATP-fueled protease and chaperone. Hence, Pln is the first chaperone identified in fungal peroxisomes. In cells of a PLN deletion strain peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. We show that this enzyme is sensitive to oxidative damage. The oxidatively damaged, but not the native protein, is a substrate of the Pln protease. Cells of the pln strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. Together with the observation that Pln has chaperone activity in vitro, our data suggest that catalase-peroxidase aggregates accumulate in peroxisomes of pln cells due to the combined absence of Pln protease and chaperone activities.

Original languageEnglish
Pages (from-to)27380-27395
Number of pages16
JournalThe Journal of Biological Chemistry
Volume287
Issue number33
Publication statusPublished - 10-Aug-2012

    Keywords

  • RAY SOLUTION SCATTERING, SMALL-ANGLE SCATTERING, PENICILLIUM-CHRYSOGENUM, HANSENULA-POLYMORPHA, SACCHAROMYCES-CEREVISIAE, MOLECULAR CHAPERONES, CITRATE SYNTHASE, HIGH-RESOLUTION, MATRIX PROTEIN, IN-VITRO

Download statistics

No data available

ID: 5649021