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Changes in specific protein degradation rates in Arabidopsis thaliana reveal multiple roles of Lon1 in mitochondrial protein homeostasis
Author(s) -
Li Lei,
Nelson Clark,
Fenske Ricarda,
Trösch Josua,
Pružinská Adriana,
Millar A. Harvey,
Huang Shaobai
Publication year - 2017
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13392
Subject(s) - biochemistry , protein degradation , prohibitin , enzyme , ribosomal protein , mitochondrion , biology , proteome , ribosome , rna , gene
Summary Mitochondrial Lon1 loss impairs oxidative phosphorylation complexes and TCA enzymes and causes accumulation of specific mitochondrial proteins. Analysis of over 400 mitochondrial protein degradation rates using 15 N labelling showed that 205 were significantly different between wild type ( WT ) and lon1‐1 . Those proteins included ribosomal proteins, electron transport chain subunits and TCA enzymes. For respiratory complexes I and V, decreased protein abundance correlated with higher degradation rate of subunits in total mitochondrial extracts. After blue native separation, however, the assembled complexes had slow degradation, while smaller subcomplexes displayed rapid degradation in lon1‐1 . In insoluble fractions, a number of TCA enzymes were more abundant but the proteins degraded slowly in lon1‐1 . In soluble protein fractions, TCA enzymes were less abundant but degraded more rapidly. These observations are consistent with the reported roles of Lon1 as a chaperone aiding the proper folding of newly synthesized/imported proteins to stabilise them and as a protease to degrade mitochondrial protein aggregates. HSP 70, prohibitin and enzymes of photorespiration accumulated in lon1‐1 and degraded slowly in all fractions, indicating an important role of Lon1 in their clearance from the proteome.