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Release of a nuclear ubiquitin-like protein activates proteasomal degradation of mislocalized hydrophobic mitochondrial proteins in trypanosomes

ABSTRACT: Mitochondrial protein import in the parasitic protozoan Trypanosoma brucei is mediated by the atypical outer membrane translocase ATOM. It consists of seven subunits including ATOM69, the import receptor for hydrophobic proteins. Ablation of ATOM69, but not of any other subunit, triggers a unique quality control pathway resulting in the proteasomal degradation of non-imported mitochondrial proteins. The process requires a protein of unknown function, an E3 ubiquitin ligase and the ubiquitin-like protein (TbUbL1), which all are recruited to the mitochondrion upon ATOM69 depletion. TbUbL1 is a nuclear protein, a fraction of which is released to the cytosol upon triggering of the pathway. Nuclear release is essential since cytosolic TbUbL1 can bind mislocalized mitochondrial proteins and likely transfers them to the proteasome. Mitochondrial quality control has previously been studied in yeast and metazoans. Finding such a pathway in the highly diverged trypanosomes suggests such pathways are an obligate feature of all mitochondria.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Trypanosoma Brucei

SUBMITTER: Friedel Drepper

LAB HEAD: Bettina Warscheid

PROVIDER: PXD027652 | Pride | 2022-05-04

REPOSITORIES: Pride

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			Action	DRS
	QEplus022094.raw	Raw
	QEplus022095.raw	Raw
	QEplus022097.raw	Raw
	QEplus022100.raw	Raw
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