Home > Research > Publications & Outputs > Trypanosomal TAC40 constitutes a novel subclass...

Research

Links

Text available via DOI:

View graph of relations

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

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance. / Schnarwiler, Felix; Niemann, Moritz; Doiron, Nicholas et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 111, No. 21, 27.05.2014, p. 7624-7629.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Schnarwiler, F, Niemann, M, Doiron, N, Harsman, A, Kaeser, S, Mani, J, Chanfon, A, Dewar, CE, Oeljeklaus, S, Jackson, CB, Pusnik, M, Schmidt, O, Meisinger, C, Hiller, S, Warscheid, B, Schnaufer, AC, Ochsenreiter, T & Schneider, A 2014, 'Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance', Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 21, pp. 7624-7629. https://doi.org/10.1073/PNAS.1404854111

APA

Schnarwiler, F., Niemann, M., Doiron, N., Harsman, A., Kaeser, S., Mani, J., Chanfon, A., Dewar, C. E., Oeljeklaus, S., Jackson, C. B., Pusnik, M., Schmidt, O., Meisinger, C., Hiller, S., Warscheid, B., Schnaufer, A. C., Ochsenreiter, T., & Schneider, A. (2014). Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance. Proceedings of the National Academy of Sciences of the United States of America, 111(21), 7624-7629. https://doi.org/10.1073/PNAS.1404854111

Vancouver

Schnarwiler F, Niemann M, Doiron N, Harsman A, Kaeser S, Mani J et al. Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance. Proceedings of the National Academy of Sciences of the United States of America. 2014 May 27;111(21):7624-7629. Epub 2014 May 12. doi: 10.1073/PNAS.1404854111

Author

Schnarwiler, Felix ; Niemann, Moritz ; Doiron, Nicholas et al. / Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance. In: Proceedings of the National Academy of Sciences of the United States of America. 2014 ; Vol. 111, No. 21. pp. 7624-7629.

Bibtex

@article{7ea5937d4ae34f05b8dfc528948ad386,
title = "Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance",
abstract = "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.",
author = "Felix Schnarwiler and Moritz Niemann and Nicholas Doiron and Anke Harsman and Sandro Kaeser and Jan Mani and Astrid Chanfon and Dewar, {Caroline E.} and Silke Oeljeklaus and Jackson, {Christopher B.} and Mascha Pusnik and Oliver Schmidt and Chris Meisinger and Sebastian Hiller and Bettina Warscheid and Schnaufer, {Achim C.} and Torsten Ochsenreiter and Andre Schneider",
year = "2014",
month = may,
day = "27",
doi = "10.1073/PNAS.1404854111",
language = "English",
volume = "111",
pages = "7624--7629",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "21",

}

RIS

TY - JOUR

T1 - Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance

AU - Schnarwiler, Felix

AU - Niemann, Moritz

AU - Doiron, Nicholas

AU - Harsman, Anke

AU - Kaeser, Sandro

AU - Mani, Jan

AU - Chanfon, Astrid

AU - Dewar, Caroline E.

AU - Oeljeklaus, Silke

AU - Jackson, Christopher B.

AU - Pusnik, Mascha

AU - Schmidt, Oliver

AU - Meisinger, Chris

AU - Hiller, Sebastian

AU - Warscheid, Bettina

AU - Schnaufer, Achim C.

AU - Ochsenreiter, Torsten

AU - Schneider, Andre

PY - 2014/5/27

Y1 - 2014/5/27

N2 - 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.

AB - 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.

UR - https://publons.com/wos-op/publon/5854545/

U2 - 10.1073/PNAS.1404854111

DO - 10.1073/PNAS.1404854111

M3 - Journal article

VL - 111

SP - 7624

EP - 7629

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 21

ER -