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Delayed degradation of chlorophylls and photosynthetic proteins in Arabidopsis autophagy mutants during stress-induced leaf yellowing.

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Sakuraba Yasuhito, Lee Sang-Hwa, Kim Ye-Sol, Park Ohkmae K, Hörtensteiner Stefan, Paek Nam-Chon,
Project Chlorophyll breakdown: catabolite modification and transport, and the relation to stoma function and cell death signalling
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Original article (peer-reviewed)

Journal Journal of experimental botany
Volume (Issue) 65(14)
Page(s) 3915 - 25
Title of proceedings Journal of experimental botany
DOI 10.1093/jxb/eru008

Open Access

Type of Open Access Publisher (Gold Open Access)


Plant autophagy, one of the essential proteolysis systems, balances proteome and nutrient levels in cells of the whole plant. Autophagy has been studied by analysing Arabidopsis thaliana autophagy-defective atg mutants, but the relationship between autophagy and chlorophyll (Chl) breakdown during stress-induced leaf yellowing remains unclear. During natural senescence or under abiotic-stress conditions, extensive cell death and early yellowing occurs in the leaves of atg mutants. A new finding is revealed that atg5 and atg7 mutants exhibit a functional stay-green phenotype under mild abiotic-stress conditions, but leaf yellowing proceeds normally in wild-type leaves under these conditions. Under mild salt stress, atg5 leaves retained high levels of Chls and all photosystem proteins and maintained a normal chloroplast structure. Furthermore, a double mutant of atg5 and non-functional stay-green nonyellowing1-1 (atg5 nye1-1) showed a much stronger stay-green phenotype than either single mutant. Taking these results together, it is proposed that autophagy functions in the non-selective catabolism of Chls and photosynthetic proteins during stress-induced leaf yellowing, in addition to the selective degradation of Chl-apoprotein complexes in the chloroplasts through the senescence-induced STAY-GREEN1/NYE1 and Chl catabolic enzymes.