Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone.
J Biol Chem
; 287(33): 27380-95, 2012 Aug 10.
Article
em En
| MEDLINE
| ID: mdl-22733816
ABSTRACT
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Penicillium chrysogenum
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Proteínas Fúngicas
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Chaperonas Moleculares
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Peroxissomos
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Endopeptidases Dependentes de ATP
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article