title: Disrupting autophagy restores peroxisome function to an Arabidopsis lon2 mutant and reveals a role for the LON2 protease in peroxisomal matrix protein degradation.
abstract: Peroxisomes house critical metabolic reactions that are essential for seedling development. As seedlings mature, metabolic requirements change, and peroxisomal contents are remodeled. The resident peroxisomal protease LON2 is positioned to degrade obsolete or damaged peroxisomal proteins, but data supporting such a role in plants have remained elusive. Arabidopsis thaliana lon2 mutants display defects in peroxisomal metabolism and matrix protein import but appear to degrade matrix proteins normally. To elucidate LON2 functions, we executed a forward-genetic screen for lon2 suppressors, which revealed multiple mutations in key autophagy genes. Disabling core autophagy-related gene (ATG) products prevents autophagy, a process through which cytosolic constituents, including organelles, can be targeted for vacuolar degradation. We found that atg2, atg3, and atg7 mutations suppressed lon2 defects in auxin metabolism and matrix protein processing and rescued the abnormally large size and small number of lon2 peroxisomes. Moreover, analysis of lon2 atg mutants uncovered an apparent role for LON2 in matrix protein turnover. Our data suggest that LON2 facilitates matrix protein degradation during peroxisome content remodeling, provide evidence for the existence of pexophagy in plants, and indicate that peroxisome destruction via autophagy is enhanced when LON2 is absent.
authors.affiliation: Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005.
authors.forename: Lisa M
authors.initials: LM
authors.lastname: Farmer
authors.forename: Mauro A
authors.initials: MA
authors.lastname: Rinaldi
authors.forename: Pierce G
authors.initials: PG
authors.lastname: Young
authors.forename: Charles H
authors.initials: CH
authors.lastname: Danan
authors.forename: Sarah E
authors.initials: SE
authors.lastname: Burkhart
authors.forename: Bonnie
authors.initials: B
authors.lastname: Bartel
mesh_terms: D000626:Aminopeptidases / Q000235:genetics / Q000378:metabolism; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001343:Autophagy / Q000235:genetics*; D000071183:Autophagy-Related Proteins; D007210:Indoleacetic Acids / Q000378:metabolism; D009154:Mutation; D020675:Peroxisomes / Q000378:metabolism*; D059748:Proteolysis; D057057:Serine Proteases / Q000235:genetics / Q000378:metabolism*; D044764:Ubiquitin-Activating Enzymes
chemical_list: D000626:Aminopeptidases; D029681:Arabidopsis Proteins; D000071183:Autophagy-Related Proteins; D007210:Indoleacetic Acids; D057057:Serine Proteases; C491970:APG7 protein, Arabidopsis; D044764:Ubiquitin-Activating Enzymes; C518661:Atg2 protein, Arabidopsis