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

Autor(en): Becker, Thomas
Wenz, Lena-Sophie
Krueger, Vivien
Lehmann, Waltraut
Mueller, Judith M.
Goroncy, Luise
Zufall, Nicole
Lithgow, Trevor
Guiard, Bernard
Chacinska, Agnieszka
Wagner, Richard 
Meisinger, Chris
Pfanner, Nikolaus
Stichwörter: ANCHORED PROTEINS; Cell Biology; FUSION; INSERTION PATHWAY; PORE; PREPROTEIN TRANSLOCASE; RECEPTORS TOM20; RECOGNITION; SACCHAROMYCES-CEREVISIAE; TOM COMPLEX; YEAST
Erscheinungsdatum: 2011
Herausgeber: ROCKEFELLER UNIV PRESS
Enthalten in: JOURNAL OF CELL BIOLOGY
Band: 194
Ausgabe: 3
Startseite: 387
Seitenende: 395
Zusammenfassung: 
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 beta-barrel proteins of the outer membrane. Several alpha-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.-helical outer membrane proteins with multiple transmembrane segments.
ISSN: 00219525
DOI: 10.1083/jcb.201102044

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