Proteomics

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QUATERNARY AND QUINARY ORGANIZATION OF RESPIRATORY COMPLEX SUBUNITS TO ADAPT PROTEOSTASIS-STRESS

ABSTRACT: Phase separation and reversible aggregation of proteins is a well-recognized adaptive strategy to survive stress. Here, we show that RCC subunits are engaged into improved super-quaternary organizations inside mitochondria during proteostasis stress. Assembly and oligomeric organizations of Complex II and V are consolidated while Complex I, III and IV are increasingly incorporated into respiratory supercomplexes in multiple cell-lines with different proteostasis and metabolic demands. Further, our results suggest that improved supra-organization of respiratory complexes (iSRC) is an outcome of conformational optimization towards better enzyme activity and co-terminus to appearance of aggregates of RCC subunits in stressed cells. Simultaneous reversion of iSRC and disappearance of the aggregates during stress-withdrawal indicates complementarity between these quaternary and quinary proteome-reorganization mechanisms. iSRC appears to be the pre-emptive and deterministic ensemble over stochastic aggregation as it offers direct fitness-benefit.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Swasti Raychaudhuri  

LAB HEAD: Swasti Raychaudhuri

PROVIDER: PXD014361 | Pride | 2024-04-04

REPOSITORIES: Pride

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Increased supraorganization of respiratory complexes is a dynamic multistep remodelling in response to proteostasis stress.

Rawat Shivali S   Ghosh Suparna S   Mondal Debodyuti D   Anusha Valpadashi V   Raychaudhuri Swasti S  

Journal of cell science 20200924 18

Proteasome-mediated degradation of misfolded proteins prevents aggregation inside and outside mitochondria. But how do cells safeguard the mitochondrial proteome and mitochondrial functions despite increased aggregation during proteasome inactivation? Here, using a novel two-dimensional complexome profiling strategy, we report increased supraorganization of respiratory complexes (RCs) in proteasome-inhibited cells that occurs simultaneously with increased pelletable aggregation of RC subunits in  ...[more]

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