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Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase
Members of the twin Cx(9)C protein family constitute the largest group of proteins in the intermembrane space (IMS) of mitochondria. Despite their conserved nature and their essential role in the biogenesis of the respiratory chain, the molecular function of twin Cx(9)C proteins is largely unknown....
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571295/ https://www.ncbi.nlm.nih.gov/pubmed/25926683 http://dx.doi.org/10.1091/mbc.E14-11-1526 |
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author | Bode, Manuela Woellhaf, Michael W. Bohnert, Maria van der Laan, Martin Sommer, Frederik Jung, Martin Zimmermann, Richard Schroda, Michael Herrmann, Johannes M. |
author_facet | Bode, Manuela Woellhaf, Michael W. Bohnert, Maria van der Laan, Martin Sommer, Frederik Jung, Martin Zimmermann, Richard Schroda, Michael Herrmann, Johannes M. |
author_sort | Bode, Manuela |
collection | PubMed |
description | Members of the twin Cx(9)C protein family constitute the largest group of proteins in the intermembrane space (IMS) of mitochondria. Despite their conserved nature and their essential role in the biogenesis of the respiratory chain, the molecular function of twin Cx(9)C proteins is largely unknown. We performed a SILAC-based quantitative proteomic analysis to identify interaction partners of the conserved twin Cx(9)C protein Cox19. We found that Cox19 interacts in a dynamic manner with Cox11, a copper transfer protein that facilitates metalation of the Cu(B) center of subunit 1 of cytochrome c oxidase. The interaction with Cox11 is critical for the stable accumulation of Cox19 in mitochondria. Cox19 consists of a helical hairpin structure that forms a hydrophobic surface characterized by two highly conserved tyrosine-leucine dipeptides. These residues are essential for Cox19 function and its specific binding to a cysteine-containing sequence in Cox11. Our observations suggest that an oxidative modification of this cysteine residue of Cox11 stimulates Cox19 binding, pointing to a redox-regulated interplay of Cox19 and Cox11 that is critical for copper transfer in the IMS and thus for biogenesis of cytochrome c oxidase. |
format | Online Article Text |
id | pubmed-4571295 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-45712952015-09-29 Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase Bode, Manuela Woellhaf, Michael W. Bohnert, Maria van der Laan, Martin Sommer, Frederik Jung, Martin Zimmermann, Richard Schroda, Michael Herrmann, Johannes M. Mol Biol Cell Articles Members of the twin Cx(9)C protein family constitute the largest group of proteins in the intermembrane space (IMS) of mitochondria. Despite their conserved nature and their essential role in the biogenesis of the respiratory chain, the molecular function of twin Cx(9)C proteins is largely unknown. We performed a SILAC-based quantitative proteomic analysis to identify interaction partners of the conserved twin Cx(9)C protein Cox19. We found that Cox19 interacts in a dynamic manner with Cox11, a copper transfer protein that facilitates metalation of the Cu(B) center of subunit 1 of cytochrome c oxidase. The interaction with Cox11 is critical for the stable accumulation of Cox19 in mitochondria. Cox19 consists of a helical hairpin structure that forms a hydrophobic surface characterized by two highly conserved tyrosine-leucine dipeptides. These residues are essential for Cox19 function and its specific binding to a cysteine-containing sequence in Cox11. Our observations suggest that an oxidative modification of this cysteine residue of Cox11 stimulates Cox19 binding, pointing to a redox-regulated interplay of Cox19 and Cox11 that is critical for copper transfer in the IMS and thus for biogenesis of cytochrome c oxidase. The American Society for Cell Biology 2015-07-01 /pmc/articles/PMC4571295/ /pubmed/25926683 http://dx.doi.org/10.1091/mbc.E14-11-1526 Text en © 2015 Bode 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 for Cell Biology. |
spellingShingle | Articles Bode, Manuela Woellhaf, Michael W. Bohnert, Maria van der Laan, Martin Sommer, Frederik Jung, Martin Zimmermann, Richard Schroda, Michael Herrmann, Johannes M. Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
title | Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
title_full | Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
title_fullStr | Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
title_full_unstemmed | Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
title_short | Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
title_sort | redox-regulated dynamic interplay between cox19 and the copper-binding protein cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571295/ https://www.ncbi.nlm.nih.gov/pubmed/25926683 http://dx.doi.org/10.1091/mbc.E14-11-1526 |
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