Homologue replacement in the import motor of the mitochondrial inner membrane of trypanosomes

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Abstract

Many mitochondrial proteins contain N-terminal presequences that direct them to the organelle. The main driving force for their translocation across the inner membrane is provided by the presequence translocase-associated motor (PAM) which contains the J-protein Pam18. Here, we show that in the PAM of Trypanosoma brucei the function of Pam18 has been replaced by the non-orthologous euglenozoan-specific J-protein TbPam27. TbPam27 is specifically required for the import of mitochondrial presequence-containing but not for carrier proteins. Similar to yeast Pam18, TbPam27 requires an intact J-domain to function. Surprisingly, T. brucei still contains a bona fide Pam18 orthologue that, while essential for normal growth, is not involved in protein import. Thus, during evolution of kinetoplastids, Pam18 has been replaced by TbPam27. We propose that this replacement is linked to the transition from two ancestral and functionally distinct TIM complexes, found in most eukaryotes, to the single bifunctional TIM complex present in trypanosomes.

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All produced data are contained within the manuscript (e.g. Data Source files)

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Corinne von Känel

Department of Chemistry and Biochemistry, University of Berne, Bern, Switzerland

Competing interests
The authors declare that no competing interests exist.
Sergio A Muñoz-Gómez

Center for Mechanisms of Evolution, Arizona State University, Arizona, United States

Competing interests
The authors declare that no competing interests exist.
Silke Oeljeklaus

Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Freiburg, Germany

Competing interests
The authors declare that no competing interests exist.
Christoph Wenger

Department of Chemistry and Biochemistry, University of Berne, Bern, Switzerland

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The authors declare that no competing interests exist.
Bettina Warscheid

Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Freiburg, Germany

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The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0001-5096-1975
Jeremy G Wideman

Center for Mechanisms of Evolution, Biodesign Institute, Arizona State University, Tempe, United States

For correspondence
Jeremy.Wideman@asu.edu

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The authors declare that no competing interests exist.
Anke Harsman

Department of Chemistry and Biochemistry, University of Berne, Bern, Switzerland

For correspondence
anke.harsman@web.de

Competing interests
The authors declare that no competing interests exist.
Andre Schneider

Department of Chemistry and Biochemistry, University of Berne, Bern, Switzerland

For correspondence
andre.schneider@dcb.unibe.ch

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0001-5421-0909

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (175563)

Andre Schneider

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (NCCR RNA and Disease)

Andre Schneider

ERC Consolidator grant (648235)

Bettina Warscheid

Deutsche Forschungsgemeinschaft (403222702/SFB 1381)

Bettina Warscheid

Germany's Excellence Strategy (CIBSS - EXC-2189 - Project ID 390939984)

Bettina Warscheid

Excellence Initiative of the German Federal and State Governments (EXC 294 BIOSS)

Bettina Warscheid

Peter und Traudl Engelhorn foundation

Anke Harsman

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

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This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.