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Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex

The mitochondrial outer membrane contains proteinaceous machineries for the translocation of precursor proteins. The sorting and assembly machinery (SAM) is required for the insertion of β‑barrel proteins into the outer membrane. Sam50 is the channel-forming core subunit of the SAM complex and belon...

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Autores principales: Stroud, David A., Becker, Thomas, Qiu, Jian, Stojanovski, Diana, Pfannschmidt, Sylvia, Wirth, Christophe, Hunte, Carola, Guiard, Bernard, Meisinger, Chris, Pfanner, Nikolaus, Wiedemann, Nils
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3154879/
https://www.ncbi.nlm.nih.gov/pubmed/21680715
http://dx.doi.org/10.1091/mbc.E11-02-0148
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author Stroud, David A.
Becker, Thomas
Qiu, Jian
Stojanovski, Diana
Pfannschmidt, Sylvia
Wirth, Christophe
Hunte, Carola
Guiard, Bernard
Meisinger, Chris
Pfanner, Nikolaus
Wiedemann, Nils
author_facet Stroud, David A.
Becker, Thomas
Qiu, Jian
Stojanovski, Diana
Pfannschmidt, Sylvia
Wirth, Christophe
Hunte, Carola
Guiard, Bernard
Meisinger, Chris
Pfanner, Nikolaus
Wiedemann, Nils
author_sort Stroud, David A.
collection PubMed
description The mitochondrial outer membrane contains proteinaceous machineries for the translocation of precursor proteins. The sorting and assembly machinery (SAM) is required for the insertion of β‑barrel proteins into the outer membrane. Sam50 is the channel-forming core subunit of the SAM complex and belongs to the BamA/Sam50/Toc75 family of proteins that have been conserved from Gram-negative bacteria to mitochondria and chloroplasts. These proteins contain one or more N-terminal polypeptide transport-associated (POTRA) domains. POTRA domains can bind precursor proteins, however, different views exist on the role of POTRA domains in the biogenesis of β-barrel proteins. It has been suggested that the single POTRA domain of mitochondrial Sam50 plays a receptor-like function at the SAM complex. We established a system to monitor the interaction of chemical amounts of β-barrel precursor proteins with the SAM complex of wild-type and mutant yeast in organello. We report that the SAM complex lacking the POTRA domain of Sam50 efficiently binds β-barrel precursors, but is impaired in the release of the precursors. These results indicate the POTRA domain of Sam50 is not essential for recognition of β-barrel precursors but functions in a subsequent step to promote the release of precursor proteins from the SAM complex.
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spelling pubmed-31548792011-10-30 Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex Stroud, David A. Becker, Thomas Qiu, Jian Stojanovski, Diana Pfannschmidt, Sylvia Wirth, Christophe Hunte, Carola Guiard, Bernard Meisinger, Chris Pfanner, Nikolaus Wiedemann, Nils Mol Biol Cell Articles The mitochondrial outer membrane contains proteinaceous machineries for the translocation of precursor proteins. The sorting and assembly machinery (SAM) is required for the insertion of β‑barrel proteins into the outer membrane. Sam50 is the channel-forming core subunit of the SAM complex and belongs to the BamA/Sam50/Toc75 family of proteins that have been conserved from Gram-negative bacteria to mitochondria and chloroplasts. These proteins contain one or more N-terminal polypeptide transport-associated (POTRA) domains. POTRA domains can bind precursor proteins, however, different views exist on the role of POTRA domains in the biogenesis of β-barrel proteins. It has been suggested that the single POTRA domain of mitochondrial Sam50 plays a receptor-like function at the SAM complex. We established a system to monitor the interaction of chemical amounts of β-barrel precursor proteins with the SAM complex of wild-type and mutant yeast in organello. We report that the SAM complex lacking the POTRA domain of Sam50 efficiently binds β-barrel precursors, but is impaired in the release of the precursors. These results indicate the POTRA domain of Sam50 is not essential for recognition of β-barrel precursors but functions in a subsequent step to promote the release of precursor proteins from the SAM complex. The American Society for Cell Biology 2011-08-15 /pmc/articles/PMC3154879/ /pubmed/21680715 http://dx.doi.org/10.1091/mbc.E11-02-0148 Text en © 2011 Stroud et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Stroud, David A.
Becker, Thomas
Qiu, Jian
Stojanovski, Diana
Pfannschmidt, Sylvia
Wirth, Christophe
Hunte, Carola
Guiard, Bernard
Meisinger, Chris
Pfanner, Nikolaus
Wiedemann, Nils
Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
title Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
title_full Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
title_fullStr Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
title_full_unstemmed Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
title_short Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
title_sort biogenesis of mitochondrial β-barrel proteins: the potra domain is involved in precursor release from the sam complex
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3154879/
https://www.ncbi.nlm.nih.gov/pubmed/21680715
http://dx.doi.org/10.1091/mbc.E11-02-0148
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