The morphology proteins Mdm12/Mmm1 function in the major [beta]-barrel assembly pathway of mitochondria

The beta-barrel proteins of mitochondria are synthesized on cytosolic ribosomes. The proteins are imported by the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM). It has been assumed that the SAM(core) complex with the subunits Sam35, Sam37 and Sam50 represents t...

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Bibliographic Details
Published in:The EMBO journal 2007-05, Vol.26 (9), p.2229
Main Authors: Meisinger, Chris, Pfannschmidt, Sylvia, Rissler, Michael, Milenkovic, Dusanka, Becker, Thomas, Stojanovski, Diana, Youngman, Matthew J, Jensen, Robert E, Chacinska, Agnieszka, Guiard, Bernard, Pfanner, Nikolaus, Wiedemann, Nils
Format: Article
Language:English
Subjects:
Membranes
Molecular biology
Molecular structure
Proteins
Online Access:Get full text
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Summary:The beta-barrel proteins of mitochondria are synthesized on cytosolic ribosomes. The proteins are imported by the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM). It has been assumed that the SAM(core) complex with the subunits Sam35, Sam37 and Sam50 represents the last import stage common to all beta-barrel proteins, followed by splitting in a Tom40-specific route and a route for other beta-barrel proteins. We have identified new components of the beta-barrel assembly machinery and show that the major beta-barrel pathway extends beyond SAM(core). Mdm12/Mmm1 function after SAM(core) yet before splitting of the major pathway. Mdm12/Mmm1 have been known for their role in maintenance of mitochondrial morphology but we reveal assembly of beta-barrel proteins as their primary function. Moreover, Mdm10, which functions in the Tom40-specific route, can associate with SAM(core) as well as Mdm12/Mmm1 to form distinct assembly complexes, indicating a dynamic exchange between the machineries governing mitochondrial beta-barrel assembly. We conclude that assembly of mitochondrial beta-barrel proteins represents a major function of the morphology proteins Mdm12/Mmm1.
ISSN:0261-4189
1460-2075
DOI:10.1038/sj.emboj.7601673