The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins

Author:

Becker Thomas1,Wenz Lena-Sophie11,Krüger Vivien12,Lehmann Waltraut1,Müller Judith M.11,Goroncy Luise1,Zufall Nicole1,Lithgow Trevor3,Guiard Bernard4,Chacinska Agnieszka15,Wagner Richard2,Meisinger Chris11,Pfanner Nikolaus11

Affiliation:

1. Institute for Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Biology, and Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany

2. Abteilung Biophysik, Fachbereich Biologie/Chemie, Universität Osnabrück, 49034 Osnabrück, Germany

3. Department of Biochemistry and Molecular Biology, Monash University, Melbourne 3800, Australia

4. Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France

5. International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland

Abstract

The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the outer membrane. Several α-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of α-helical outer membrane proteins with multiple transmembrane segments.

Publisher

Rockefeller University Press

Subject

Cell Biology

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