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

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

  • von Känel, Corinne ORCID Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
  • Muñoz-Gómez, Sergio A Center for Mechanisms of Evolution, Biodesign Institute, School of Life Sciences, Arizona State University, Tempe, United States
  • Oeljeklaus, Silke Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, Germany
  • Wenger, Christoph Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
  • Warscheid, Bettina ORCID Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, Germany
  • Wideman, Jeremy G Center for Mechanisms of Evolution, Biodesign Institute, School of Life Sciences, Arizona State University, Tempe, United States
  • Harsman, Anke Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
  • Schneider, Andre ORCID Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
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  • 2020-2-27
Published in:
  • eLife. - eLife Sciences Publications, Ltd. - 2020, vol. 9
General Biochemistry, Genetics and Molecular Biology
General Immunology and Microbiology
General Neuroscience
General Medicine
English 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 Here, we show that in the PAM of Trypanosoma brucei the function of Pam18 has been replaced by the non-orthologous euglenozoan-specific J-protein TbPam27.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 Thus, during evolution of kinetoplastids, Pam18 has been replaced by TbPam27.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.
Language
  • English
Open access status
gold
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Persistent URL
https://sonar.ch/global/documents/206225
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