Trypanosomal TAC40 constitutes a novel subclass of mitochondrial -barrel proteins specialized in mitochondrial genome inheritance

Schnarwiler, Felix; Niemann, Moritz; Doiron, Nicholas; Harsman, Anke Judith; Käser, Sandro; Mani, Jan; Chanfon, Astrid; Dewar, C. E.; Oeljeklaus, S.; Jackson, Christopher; Pusnik, M.; Schmidt, O.; Meisinger, C.; Hiller, S.; Warscheid, B.; Schnaufer, A. C.; Ochsenreiter, Torsten; Schneider, André (2014). Trypanosomal TAC40 constitutes a novel subclass of mitochondrial -barrel proteins specialized in mitochondrial genome inheritance. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 111(21), pp. 7624-7629. National Academy of Sciences NAS 10.1073/pnas.1404854111

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Mitochondria cannot form de novo but require mechanisms allowing their inheritance to daughter cells. In contrast to most other eukaryotes Trypanosoma brucei has a single mitochondrion whose single-unit genome is physically connected to the flagellum. Here we identify a β-barrel mitochondrial outer membrane protein, termed tripartite attachment complex 40 (TAC40), that localizes to this connection. TAC40 is essential for mitochondrial DNA inheritance and belongs to the mitochondrial porin protein family. However, it is not specifically related to any of the three subclasses of mitochondrial porins represented by the metabolite transporter voltage-dependent anion channel (VDAC), the protein translocator of the outer membrane 40 (TOM40), or the fungi-specific MDM10, a component of the endoplasmic reticulum–mitochondria encounter structure (ERMES). MDM10 and TAC40 mediate cellular architecture and participate in transmembrane complexes that are essential for mitochondrial DNA inheritance. In yeast MDM10, in the context of the ERMES, is postulated to connect the mitochondrial genomes to actin filaments, whereas in trypanosomes TAC40 mediates the linkage of the mitochondrial DNA to the basal body of the flagellum. However, TAC40 does not colocalize with trypanosomal orthologs of ERMES components and, unlike MDM10, it regulates neither mitochondrial morphology nor the assembly of the protein translocase. TAC40 therefore defines a novel subclass of mitochondrial porins that is distinct from VDAC, TOM40, and MDM10. However, whereas the architecture of the TAC40-containing complex in trypanosomes and the MDM10-containing ERMES in yeast is very different, both are organized around a β-barrel protein of the mitochondrial porin family that mediates a DNA–cytoskeleton linkage that is essential for mitochondrial DNA inheritance.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Cell Biology
04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Institute of Clinical Chemistry
08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Schnarwiler, Felix; Niemann, Moritz; Doiron, Nicholas; Harsman, Anke Judith; Käser, Sandro; Mani, Jan; Chanfon, Astrid; Jackson, Christopher; Ochsenreiter, Torsten and Schneider, André

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health
500 Science > 540 Chemistry

ISSN:

0027-8424

Publisher:

National Academy of Sciences NAS

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

25 Jun 2014 09:38

Last Modified:

10 Aug 2015 15:35

Publisher DOI:

10.1073/pnas.1404854111

PubMed ID:

24821793

BORIS DOI:

10.7892/boris.52636

URI:

https://boris.unibe.ch/id/eprint/52636

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