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Role of the small protein Mco6 in the mitochondrial sorting and assembly machinery.
Busto, Jon V; Ganesan, Iniyan; Mathar, Hannah; Steiert, Conny; Schneider, Eva F; Straub, Sebastian P; Ellenrieder, Lars; Song, Jiyao; Stiller, Sebastian B; Lübbert, Philipp; Chatterjee, Ritwika; Elsaesser, Jana; Melchionda, Laura; Schug, Christina; den Brave, Fabian; Schulte, Uwe; Klecker, Till; Kraft, Claudine; Fakler, Bernd; Becker, Thomas; Wiedemann, Nils.
  • Busto JV; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Ganesan I; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Mathar H; Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany.
  • Steiert C; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Schneider EF; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Straub SP; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; Faculty of Biology, University of Freiburg, Freiburg, Germany.
  • Ellenrieder L; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Song J; Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany.
  • Stiller SB; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Lübbert P; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Chatterjee R; Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany.
  • Elsaesser J; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; Faculty of Biology, University of Freiburg, Freiburg, Germany.
  • Melchionda L; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
  • Schug C; Institute of Cell Biology, University of Bayreuth, Bayreuth, Germany.
  • den Brave F; Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany.
  • Schulte U; Institute of Physiology, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
  • Klecker T; Institute of Cell Biology, University of Bayreuth, Bayreuth, Germany.
  • Kraft C; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
  • Fakler B; Institute of Physiology, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany; Center for Basics in NeuroModulation, Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, Uni
  • Becker T; Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany. Electronic address: thbecker@uni-bonn.de.
  • Wiedemann N; Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freibu
Cell Rep ; 43(3): 113805, 2024 Mar 26.
Article en En | MEDLINE | ID: mdl-38377000
ABSTRACT
The majority of mitochondrial precursor proteins are imported through the Tom40 ß-barrel channel of the translocase of the outer membrane (TOM). The sorting and assembly machinery (SAM) is essential for ß-barrel membrane protein insertion into the outer membrane and thus required for the assembly of the TOM complex. Here, we demonstrate that the α-helical outer membrane protein Mco6 co-assembles with the mitochondrial distribution and morphology protein Mdm10 as part of the SAM machinery. MCO6 and MDM10 display a negative genetic interaction, and a mco6-mdm10 yeast double mutant displays reduced levels of the TOM complex. Cells lacking Mco6 affect the levels of Mdm10 and show assembly defects of the TOM complex. Thus, this work uncovers a role of the SAMMco6 complex for the biogenesis of the mitochondrial outer membrane.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Proteínas de Saccharomyces cerevisiae Idioma: En Año: 2024 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Proteínas de Saccharomyces cerevisiae Idioma: En Año: 2024 Tipo del documento: Article