Abstract
In photosynthetic cells, a large amount of hydrogen peroxide is produced in peroxisomes through photorespiration, which is a metabolic pathway related to photosynthesis. Hydrogen peroxide, a reactive oxygen species, oxidizes peroxisomal proteins and membrane lipids, resulting in a decrease in peroxisomal quality. We demonstrate that the autophagic system is responsible for the elimination of oxidized peroxisomes in plant. We isolated Arabidopsis mutants that accumulated oxidized peroxisomes, which formed large aggregates. We revealed that these mutants were defective in autophagy-related (ATG) genes and that the aggregated peroxisomes were selectively targeted by the autophagic machinery. These findings suggest that autophagy plays an important role in the quality control of peroxisomes by the selective degradation of oxidized peroxisomes. In addition, the results suggest that autophagy is also responsible for the functional transition of glyoxysomes to leaf peroxisomes.
Original language | English |
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Pages (from-to) | 936-937 |
Number of pages | 2 |
Journal | Autophagy |
Volume | 10 |
Issue number | 5 |
DOIs | |
Publication status | Published - May 2014 |
Keywords
- Arabidopsis thaliana
- Glyoxysome leaf peroxisome
- Hydrogen peroxide
- Peroxisome
- Peroxisome transition
- Pexophagy
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology