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In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins
The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase E...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469512/ https://www.ncbi.nlm.nih.gov/pubmed/22918950 http://dx.doi.org/10.1091/mbc.E12-05-0358 |
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author | Böttinger, Lena Gornicka, Agnieszka Czerwik, Tomasz Bragoszewski, Piotr Loniewska-Lwowska, Adrianna Schulze-Specking, Agnes Truscott, Kaye N. Guiard, Bernard Milenkovic, Dusanka Chacinska, Agnieszka |
author_facet | Böttinger, Lena Gornicka, Agnieszka Czerwik, Tomasz Bragoszewski, Piotr Loniewska-Lwowska, Adrianna Schulze-Specking, Agnes Truscott, Kaye N. Guiard, Bernard Milenkovic, Dusanka Chacinska, Agnieszka |
author_sort | Böttinger, Lena |
collection | PubMed |
description | The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds. It was unclear what the mechanisms are that ensure that proteins are released from Mia40 in a fully oxidized form. In this work, we dissect the stage of the oxidative folding relay, in which Mia40 binds to its substrate. We identify dynamics of the Mia40–substrate intermediate complex. Our experiments performed in a native environment, both in organello and in vivo, show that Erv1 directly participates in Mia40–substrate complex dynamics by forming a ternary complex. Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria. |
format | Online Article Text |
id | pubmed-3469512 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34695122012-12-30 In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins Böttinger, Lena Gornicka, Agnieszka Czerwik, Tomasz Bragoszewski, Piotr Loniewska-Lwowska, Adrianna Schulze-Specking, Agnes Truscott, Kaye N. Guiard, Bernard Milenkovic, Dusanka Chacinska, Agnieszka Mol Biol Cell Articles The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds. It was unclear what the mechanisms are that ensure that proteins are released from Mia40 in a fully oxidized form. In this work, we dissect the stage of the oxidative folding relay, in which Mia40 binds to its substrate. We identify dynamics of the Mia40–substrate intermediate complex. Our experiments performed in a native environment, both in organello and in vivo, show that Erv1 directly participates in Mia40–substrate complex dynamics by forming a ternary complex. Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria. The American Society for Cell Biology 2012-10-15 /pmc/articles/PMC3469512/ /pubmed/22918950 http://dx.doi.org/10.1091/mbc.E12-05-0358 Text en © 2012 Böttinger 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 BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Böttinger, Lena Gornicka, Agnieszka Czerwik, Tomasz Bragoszewski, Piotr Loniewska-Lwowska, Adrianna Schulze-Specking, Agnes Truscott, Kaye N. Guiard, Bernard Milenkovic, Dusanka Chacinska, Agnieszka In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins |
title | In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins |
title_full | In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins |
title_fullStr | In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins |
title_full_unstemmed | In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins |
title_short | In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins |
title_sort | in vivo evidence for cooperation of mia40 and erv1 in the oxidation of mitochondrial proteins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469512/ https://www.ncbi.nlm.nih.gov/pubmed/22918950 http://dx.doi.org/10.1091/mbc.E12-05-0358 |
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