Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and ChaperoneBartoszewska, 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 journal › Article › Academic › peer-review
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.
|Number of pages||16|
|Journal||The Journal of Biological Chemistry|
|Publication status||Published - 10-Aug-2012|
- RAY SOLUTION SCATTERING, SMALL-ANGLE SCATTERING, PENICILLIUM-CHRYSOGENUM, HANSENULA-POLYMORPHA, SACCHAROMYCES-CEREVISIAE, MOLECULAR CHAPERONES, CITRATE SYNTHASE, HIGH-RESOLUTION, MATRIX PROTEIN, IN-VITRO