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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...

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Autores principales: Böttinger, Lena, Gornicka, Agnieszka, Czerwik, Tomasz, Bragoszewski, Piotr, Loniewska-Lwowska, Adrianna, Schulze-Specking, Agnes, Truscott, Kaye N., Guiard, Bernard, Milenkovic, Dusanka, Chacinska, Agnieszka
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
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.
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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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