The mitochondrial import complex MIM functions as main translocase for [alpha]-helical outer membrane proteins

Abstract: The mitochondrial outer membrane contains integral proteins with a-helical membrane anchors or a transmembrane b-barrel. The translocase of the outer membrane (TOM) cooperates with the sorting and assembly machinery (SAM) in the import of b-barrel proteins, whereas the mitochondrial import (MIM) complex inserts precursors of multi-spanning a-helical proteins. Single-spanning proteins constitute more than half of the integral outer membrane proteins; however, their biogenesis is poorly understood. We report that the yeast MIM complex promotes the insertion of proteins with N-terminal (signal-anchored) or C-terminal (tailanchored) membrane anchors. The MIM complex exists in three dynamic populations. MIM interacts with TOM to accept precursor proteins from the receptor Tom70. Free MIM complexes insert single-spanning proteins that are imported in a Tom70-independent manner. Finally, coupling of MIM and SAM promotes early assembly steps of TOM subunits. We conclude that the MIM complex is a major and versatile protein translocase of the mitochondrial outer membrane

Angaben zum Objekt

• Standort: Deutsche Nationalbibliothek Frankfurt am Main
• Umfang: Online-Ressource
• Sprache: Englisch
• Anmerkungen: Cell reports. - 31, 4 (2020) , 107567, ISSN: 2211-1247

Beteiligte, Orts- und Zeitangaben

• Ereignis: Veröffentlichung
• (wo): Freiburg
• (wer): Universität
• (wann): 2020
• Urheber: Doan, Kim Nguyen ; Grevel, Alexander ; Mårtensson, Christoph U. ; Ellenrieder, Lars ; Thornton, Nicolas ; Wenz, Lena-Sophie ; Opaliński, Łukasz ; Guiard, Bernard ; Pfanner, Nikolaus ; Becker, Thomas

Weitere Informationen

• DOI: 10.1016/j.celrep.2020.107567
• URN: urn:nbn:de:bsz:25-freidok-1656045
• Rechteinformation: Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Letzte Aktualisierung: 14.08.2025, 10:57 MESZ