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Dysfunctional mitochondria trap proteins in the intermembrane space - Data set 1: proximity labelling

ABSTRACT: Mitochondria consist of hundreds of proteins which are initially synthesized in the cytosol as ‘precursors’ and imported into the organelle. The accumulation of precursors in the cytosol due to mitochondrial dysfunction compromises cellular proteostasis and is a hallmark of diseases. How cells counteract the accumulation of potentially toxic precursors in the cytosol is poorly understood. Using a proximity labeling-based assay to globally monitor the intramitochondrial location of proteins, we show, that upon mitochondrial dysfunction many mitochondrial matrix proteins are sequestered in the intermembrane space (IMS). This Mitochondrial Triage of Precursor proteins (MitoTraP) was not simply the result of a general translocation block at the level of the inner membrane. Rather, MitoTraP specifically directs a defined subgroup of matrix proteins into the IMS, most of which being constituents of the mitochondrial ribosome. Using the mitoribosomal protein Mrp17 (bS6m) as a model, we found that the targeting into the IMS prevents the mistargeting to the nucleolus and the interference with ribosome assembly. Thus, MitoTraP represents a novel, so far unknown mechanism of the eukaryotic quality control system that protects the cellular proteome against toxic effects of non-imported mitochondrial precursor proteins.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Markus Räschle

LAB HEAD: Markus Räschle

PROVIDER: PXD057245 | Pride | 2025-05-21

REPOSITORIES: Pride

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			Action	DRS
	20230629_HF1_MaRa_P0204_MR10_1.raw	Raw
	20230629_HF1_MaRa_P0204_MR10_2.raw	Raw
	20230629_HF1_MaRa_P0204_MR10_3.raw	Raw
	20230629_HF1_MaRa_P0204_MR10_4.raw	Raw
	20230629_HF1_MaRa_P0204_MR6_1.raw	Raw

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