Dewar, Caroline E; Oeljeklaus, Silke; Mani, Jan; Mühlhäuser, Wignand W D; von Känel, Corinne; Zimmermann, Johannes; Ochsenreiter, Torsten; Warscheid, Bettina; Schneider, André (2022). Mistargeting of aggregation prone mitochondrial proteins activates a nucleus-mediated posttranscriptional quality control pathway in trypanosomes. Nature Communications, 13(1), p. 3084. Springer Nature 10.1038/s41467-022-30748-z
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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 as cytosolic TbUbL1 can bind mislocalised 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 eukaryotes.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) 08 Faculty of Science > Department of Biology > Institute of Cell Biology |
UniBE Contributor: |
Dewar, Caroline Elizabeth, Mani, Jan, von Känel, Corinne, Ochsenreiter, Torsten, Schneider, André |
Subjects: |
500 Science > 570 Life sciences; biology 500 Science > 540 Chemistry |
ISSN: |
2041-1723 |
Publisher: |
Springer Nature |
Language: |
English |
Submitter: |
Pubmed Import |
Date Deposited: |
08 Jun 2022 12:28 |
Last Modified: |
05 Dec 2022 16:20 |
Publisher DOI: |
10.1038/s41467-022-30748-z |
PubMed ID: |
35654893 |
BORIS DOI: |
10.48350/170484 |
URI: |
https://boris.unibe.ch/id/eprint/170484 |
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