The non-canonical mitochondrial inner membrane presequence translocase of trypanosomatids contains two essential rhomboid-like proteins

Harsman, Anke Judith; Oeljeklaus, Silke; Wenger, Christoph; Huot, Jonathan; Warscheid, Bettina; Schneider, André (2016). The non-canonical mitochondrial inner membrane presequence translocase of trypanosomatids contains two essential rhomboid-like proteins. Nature communications, 7, p. 13707. Nature Publishing Group 10.1038/ncomms13707

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Mitochondrial protein import is essential for all eukaryotes. Here we show that the early diverging eukaryote Trypanosoma brucei has a non-canonical inner membrane (IM) protein translocation machinery. Besides TbTim17, the single member of the Tim17/22/23 family in trypanosomes, the presequence translocase contains nine subunits that co-purify in reciprocal immunoprecipitations and with a presequence-containing substrate that is trapped in the translocation channel. Two of the newly discovered subunits are rhomboid-like proteins, which are essential for growth and mitochondrial protein import. Rhomboid-like proteins were proposed to form the protein translocation pore of the ER-associated degradation system, suggesting that they may contribute to pore formation in the presequence translocase of T. brucei. Pulldown of import-arrested mitochondrial carrier protein shows that the carrier translocase shares eight subunits with the presequence translocase. This indicates that T. brucei may have a single IM translocase that with compositional variations mediates import of presequence-containing and carrier proteins.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Harsman, Anke Judith; Wenger, Christoph; Huot, Jonathan and Schneider, André

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

2041-1723

Publisher:

Nature Publishing Group

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

24 Jan 2017 09:55

Last Modified:

24 Jan 2017 09:55

Publisher DOI:

10.1038/ncomms13707

PubMed ID:

27991487

BORIS DOI:

10.7892/boris.92435

URI:

https://boris.unibe.ch/id/eprint/92435

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