Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants

被引:4
|
作者
Ghifari, Abi S. [1 ]
Murcha, Monika W. [1 ]
机构
[1] Univ Western Australia, Sch Mol Sci, 35 Stirling Highway, Perth, WA 6009, Australia
基金
澳大利亚研究理事会;
关键词
TARGETING PEPTIDE DEGRADATION; CLP PROTEASE COMPLEX; AAA PLUS PROTEASE; ARABIDOPSIS-THALIANA; PROCESSING PEPTIDASE; INTERMEMBRANE SPACE; LON PROTEASE; TURNOVER; GROWTH; PROTEINS;
D O I
10.1042/BST20220195
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mitochondrial function relies on the homeostasis and quality control of their proteome, including components of the oxidative phosphorylation (OXPHOS) pathway that generates energy in form of ATP. OXPHOS subunits are under constant exposure to reactive oxygen species due to their oxidation-reduction activities, which consequently make them prone to oxidative damage, misfolding, and aggregation. As a result, quality control mechanisms through turnover and degradation are required for maintaining mitochondrial activity. Degradation of OXPHOS subunits can be achieved through proteomic turnover or modular degradation. In this review, we present multiple protein degradation pathways in plant mitochondria. Specifically, we focus on the intricate turnover of OXPHOS subunits, prior to protein import via cytosolic proteasomal degradation and post import and assembly via intra-mitochondrial proteolysis involving multiple AAA+ proteases. Together, these proteolytic pathways maintain the activity and homeostasis of OXPHOS components.
引用
收藏
页码:1119 / 1132
页数:14
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