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J Cell Biol. 2012 Nov 12;199(4):599-611. doi: 10.1083/jcb.201207161. Epub 2012 Nov 5.

Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane.

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1
Max-Planck Institut für Biochemie, Abteilung für zelluläre Biochemie, D-82152 Martinsried, Germany.

Abstract

The TOB-SAM complex is an essential component of the mitochondrial outer membrane that mediates the insertion of β-barrel precursor proteins into the membrane. We report here its isolation and determine its size, composition, and structural organization. The complex from Neurospora crassa was composed of Tob55-Sam50, Tob38-Sam35, and Tob37-Sam37 in a stoichiometry of 1:1:1 and had a molecular mass of 140 kD. A very minor fraction of the purified complex was associated with one Mdm10 protein. Using molecular homology modeling for Tob55 and cryoelectron microscopy reconstructions of the TOB complex, we present a model of the TOB-SAM complex that integrates biochemical and structural data. We discuss our results and the structural model in the context of a possible mechanism of the TOB insertase.

PMID:
23128244
PMCID:
PMC3494861
DOI:
10.1083/jcb.201207161
[Indexed for MEDLINE]
Free PMC Article
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