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c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm
In the absence of a tight control of copper entrance into cells, bacteria have evolved different systems to control copper concentration within the cytoplasm and the periplasm. Central to these systems, the Cu(+) ATPase CopA plays a major role in copper tolerance and translocates copper from the cyt...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society of Microbiology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4600104/ https://www.ncbi.nlm.nih.gov/pubmed/26396241 http://dx.doi.org/10.1128/mBio.01007-15 |
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author | Durand, Anne Azzouzi, Asma Bourbon, Marie-Line Steunou, Anne-Soisig Liotenberg, Sylviane Maeshima, Akinori Astier, Chantal Argentini, Manuela Saito, Shingo Ouchane, Soufian |
author_facet | Durand, Anne Azzouzi, Asma Bourbon, Marie-Line Steunou, Anne-Soisig Liotenberg, Sylviane Maeshima, Akinori Astier, Chantal Argentini, Manuela Saito, Shingo Ouchane, Soufian |
author_sort | Durand, Anne |
collection | PubMed |
description | In the absence of a tight control of copper entrance into cells, bacteria have evolved different systems to control copper concentration within the cytoplasm and the periplasm. Central to these systems, the Cu(+) ATPase CopA plays a major role in copper tolerance and translocates copper from the cytoplasm to the periplasm. The fate of copper in the periplasm varies among species. Copper can be sequestered, oxidized, or released outside the cells. Here we describe the identification of CopI, a periplasmic protein present in many proteobacteria, and show its requirement for copper tolerance in Rubrivivax gelatinosus. The ΔcopI mutant is more susceptible to copper than the Cu(+) ATPase copA mutant. CopI is induced by copper, localized in the periplasm and could bind copper. Interestingly, copper affects cytochrome c membrane complexes (cbb(3) oxidase and photosystem) in both ΔcopI and copA-null mutants, but the causes are different. In the copA mutant, heme and chlorophyll synthesis are affected, whereas in ΔcopI mutant, the decrease is a consequence of impaired cytochrome c assembly. This impact on c-type cytochromes would contribute also to the copper toxicity in the periplasm of the wild-type cells when they are exposed to high copper concentrations. |
format | Online Article Text |
id | pubmed-4600104 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American Society of Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-46001042015-10-12 c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm Durand, Anne Azzouzi, Asma Bourbon, Marie-Line Steunou, Anne-Soisig Liotenberg, Sylviane Maeshima, Akinori Astier, Chantal Argentini, Manuela Saito, Shingo Ouchane, Soufian mBio Research Article In the absence of a tight control of copper entrance into cells, bacteria have evolved different systems to control copper concentration within the cytoplasm and the periplasm. Central to these systems, the Cu(+) ATPase CopA plays a major role in copper tolerance and translocates copper from the cytoplasm to the periplasm. The fate of copper in the periplasm varies among species. Copper can be sequestered, oxidized, or released outside the cells. Here we describe the identification of CopI, a periplasmic protein present in many proteobacteria, and show its requirement for copper tolerance in Rubrivivax gelatinosus. The ΔcopI mutant is more susceptible to copper than the Cu(+) ATPase copA mutant. CopI is induced by copper, localized in the periplasm and could bind copper. Interestingly, copper affects cytochrome c membrane complexes (cbb(3) oxidase and photosystem) in both ΔcopI and copA-null mutants, but the causes are different. In the copA mutant, heme and chlorophyll synthesis are affected, whereas in ΔcopI mutant, the decrease is a consequence of impaired cytochrome c assembly. This impact on c-type cytochromes would contribute also to the copper toxicity in the periplasm of the wild-type cells when they are exposed to high copper concentrations. American Society of Microbiology 2015-09-22 /pmc/articles/PMC4600104/ /pubmed/26396241 http://dx.doi.org/10.1128/mBio.01007-15 Text en Copyright © 2015 Durand et al. http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license (http://creativecommons.org/licenses/by-nc-sa/3.0/) , which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Durand, Anne Azzouzi, Asma Bourbon, Marie-Line Steunou, Anne-Soisig Liotenberg, Sylviane Maeshima, Akinori Astier, Chantal Argentini, Manuela Saito, Shingo Ouchane, Soufian c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm |
title | c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm |
title_full | c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm |
title_fullStr | c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm |
title_full_unstemmed | c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm |
title_short | c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm |
title_sort | c-type cytochrome assembly is a key target of copper toxicity within the bacterial periplasm |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4600104/ https://www.ncbi.nlm.nih.gov/pubmed/26396241 http://dx.doi.org/10.1128/mBio.01007-15 |
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