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

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 compos...

Descripción completa

Detalles Bibliográficos
Autores principales: Klein, Astrid, Israel, Lars, Lackey, Sebastian W.K., Nargang, Frank E., Imhof, Axel, Baumeister, Wolfgang, Neupert, Walter, Thomas, Dennis R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2012
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3494861/
https://www.ncbi.nlm.nih.gov/pubmed/23128244
http://dx.doi.org/10.1083/jcb.201207161
_version_ 1782249445329469440
author Klein, Astrid
Israel, Lars
Lackey, Sebastian W.K.
Nargang, Frank E.
Imhof, Axel
Baumeister, Wolfgang
Neupert, Walter
Thomas, Dennis R.
author_facet Klein, Astrid
Israel, Lars
Lackey, Sebastian W.K.
Nargang, Frank E.
Imhof, Axel
Baumeister, Wolfgang
Neupert, Walter
Thomas, Dennis R.
author_sort Klein, Astrid
collection PubMed
description 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.
format Online
Article
Text
id pubmed-3494861
institution National Center for Biotechnology Information
language English
publishDate 2012
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-34948612013-05-12 Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane Klein, Astrid Israel, Lars Lackey, Sebastian W.K. Nargang, Frank E. Imhof, Axel Baumeister, Wolfgang Neupert, Walter Thomas, Dennis R. J Cell Biol Research Articles 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. The Rockefeller University Press 2012-11-12 /pmc/articles/PMC3494861/ /pubmed/23128244 http://dx.doi.org/10.1083/jcb.201207161 Text en © 2012 Klein et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Klein, Astrid
Israel, Lars
Lackey, Sebastian W.K.
Nargang, Frank E.
Imhof, Axel
Baumeister, Wolfgang
Neupert, Walter
Thomas, Dennis R.
Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
title Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
title_full Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
title_fullStr Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
title_full_unstemmed Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
title_short Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
title_sort characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3494861/
https://www.ncbi.nlm.nih.gov/pubmed/23128244
http://dx.doi.org/10.1083/jcb.201207161
work_keys_str_mv AT kleinastrid characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT israellars characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT lackeysebastianwk characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT nargangfranke characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT imhofaxel characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT baumeisterwolfgang characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT neupertwalter characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane
AT thomasdennisr characterizationoftheinsertaseforbbarrelproteinsoftheoutermitochondrialmembrane

Ejemplares similares