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Characterization of the insertase for beta-barrel proteins of the outer mitochondrial membrane

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons79133

Klein,  Astrid
Neupert, Walter / Structure and Function of Mitochondria, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77721

Baumeister,  Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78450

Neupert,  Walter
Neupert, Walter / Structure and Function of Mitochondria, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78794

Thomas,  Dennis R.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Klein, A., Israel, L., Lackey, S. W. K., Nargang, F. E., Imhof, A., Baumeister, W., et al. (2012). Characterization of the insertase for beta-barrel proteins of the outer mitochondrial membrane. JOURNAL OF CELL BIOLOGY, 199(4), 599-611. doi:10.1083/jcb.201207161.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-000E-7A23-7
Zusammenfassung
The TOB-SAM complex is an essential component of the mitochondrial outer membrane that mediates the insertion of beta-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 minorfraction 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.