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A salvage pathway maintains highly functional respiratory complex I
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Journal Article
A salvage pathway maintains highly functional respiratory complex I
2020
Overview
Regulation of the turnover of complex I (CI), the largest mitochondrial respiratory chain complex, remains enigmatic despite huge advancement in understanding its structure and the assembly. Here, we report that the NADH-oxidizing N-module of CI is turned over at a higher rate and largely independently of the rest of the complex by mitochondrial matrix protease ClpXP, which selectively removes and degrades damaged subunits. The observed mechanism seems to be a safeguard against the accumulation of dysfunctional CI arising from the inactivation of the N-module subunits due to attrition caused by its constant activity under physiological conditions. This CI salvage pathway maintains highly functional CI through a favorable mechanism that demands much lower energetic cost than de novo synthesis and reassembly of the entire CI. Our results also identify ClpXP activity as an unforeseen target for therapeutic interventions in the large group of mitochondrial diseases characterized by the CI instability.
Maintenance and quality control of the mitochondrial respiratory chain complexes responsible for bulk energy production are unclear. Here, the authors show that the mitochondrial protease ClpXP is required for the rapid turnover of the core N-module of respiratory complex I, which happens independently of other modules in the complex.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/1
/ 13/106
/ 38/77
/ 64/60
/ 82/29
/ 82/51
/ 82/80
/ Aging
/ Animals
/ Chains
/ Electron Transport Complex I - genetics
/ Electron Transport Complex I - metabolism
/ Endopeptidase Clp - genetics
/ Endopeptidase Clp - metabolism
/ Humanities and Social Sciences
/ Mice
/ Modules
/ NADH
/ Nicotinamide adenine dinucleotide
/ Protease
/ Protein Subunits - metabolism
/ Proteins
/ Science
