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Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold β-barrel proteins and insert them into the mitochondri...

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Autores principales: Diederichs, Kathryn A., Ni, Xiaodan, Rollauer, Sarah E., Botos, Istvan, Tan, Xiaofeng, King, Martin S., Kunji, Edmund R. S., Jiang, Jiansen, Buchanan, Susan K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7335169/
https://www.ncbi.nlm.nih.gov/pubmed/32620929
http://dx.doi.org/10.1038/s41467-020-17144-1
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author Diederichs, Kathryn A.
Ni, Xiaodan
Rollauer, Sarah E.
Botos, Istvan
Tan, Xiaofeng
King, Martin S.
Kunji, Edmund R. S.
Jiang, Jiansen
Buchanan, Susan K.
author_facet Diederichs, Kathryn A.
Ni, Xiaodan
Rollauer, Sarah E.
Botos, Istvan
Tan, Xiaofeng
King, Martin S.
Kunji, Edmund R. S.
Jiang, Jiansen
Buchanan, Susan K.
author_sort Diederichs, Kathryn A.
collection PubMed
description In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold β-barrel proteins and insert them into the mitochondrial outer membrane. We report cryoEM structures of the SAM complex from Myceliophthora thermophila, which show that Sam50 forms a 16-stranded transmembrane β-barrel with a single polypeptide-transport-associated (POTRA) domain extending into the intermembrane space. Sam35 and Sam37 are located on the cytosolic side of the outer membrane, with Sam35 capping Sam50, and Sam37 interacting extensively with Sam35. Sam35 and Sam37 each adopt a GST-like fold, with no functional, structural, or sequence similarity to their bacterial counterparts. Structural analysis shows how the Sam50 β-barrel opens a lateral gate to accommodate its substrates.
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spelling pubmed-73351692020-07-09 Structural insight into mitochondrial β-barrel outer membrane protein biogenesis Diederichs, Kathryn A. Ni, Xiaodan Rollauer, Sarah E. Botos, Istvan Tan, Xiaofeng King, Martin S. Kunji, Edmund R. S. Jiang, Jiansen Buchanan, Susan K. Nat Commun Article In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold β-barrel proteins and insert them into the mitochondrial outer membrane. We report cryoEM structures of the SAM complex from Myceliophthora thermophila, which show that Sam50 forms a 16-stranded transmembrane β-barrel with a single polypeptide-transport-associated (POTRA) domain extending into the intermembrane space. Sam35 and Sam37 are located on the cytosolic side of the outer membrane, with Sam35 capping Sam50, and Sam37 interacting extensively with Sam35. Sam35 and Sam37 each adopt a GST-like fold, with no functional, structural, or sequence similarity to their bacterial counterparts. Structural analysis shows how the Sam50 β-barrel opens a lateral gate to accommodate its substrates. Nature Publishing Group UK 2020-07-03 /pmc/articles/PMC7335169/ /pubmed/32620929 http://dx.doi.org/10.1038/s41467-020-17144-1 Text en © This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Diederichs, Kathryn A.
Ni, Xiaodan
Rollauer, Sarah E.
Botos, Istvan
Tan, Xiaofeng
King, Martin S.
Kunji, Edmund R. S.
Jiang, Jiansen
Buchanan, Susan K.
Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_full Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_fullStr Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_full_unstemmed Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_short Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
title_sort structural insight into mitochondrial β-barrel outer membrane protein biogenesis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7335169/
https://www.ncbi.nlm.nih.gov/pubmed/32620929
http://dx.doi.org/10.1038/s41467-020-17144-1
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