【7/12更新】2022年4月1日からのCiNii ArticlesのCiNii Researchへの統合について

c -Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm

  • Anne Durand
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France
  • Asma Azzouzi
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France
  • Marie-Line Bourbon
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France
  • Anne-Soisig Steunou
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France
  • Sylviane Liotenberg
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France
  • Akinori Maeshima
    Graduate School of Science and Engineering, Saitama University, Shimo-Okubo, Sakura-ku, Saitama, Japan
  • Chantal Astier
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France
  • Manuela Argentini
    Institut de la Vision, UPMC Université Paris, UMR_S 968, Paris 75012, France
  • Shingo Saito
    Graduate School of Science and Engineering, Saitama University, Shimo-Okubo, Sakura-ku, Saitama, Japan
  • Soufian Ouchane
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR9198, Université Paris Sud, Gif sur Yvette 91198, France

抄録

<jats:title>ABSTRACT</jats:title> <jats:p> 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 <jats:sup>+</jats:sup> 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 <jats:named-content content-type="genus-species">Rubrivivax gelatinosus</jats:named-content> . The Δ <jats:italic>copI</jats:italic> mutant is more susceptible to copper than the Cu <jats:sup>+</jats:sup> ATPase <jats:italic>copA</jats:italic> mutant. CopI is induced by copper, localized in the periplasm and could bind copper. Interestingly, copper affects cytochrome <jats:italic>c</jats:italic> membrane complexes ( <jats:italic> cbb <jats:sub>3</jats:sub> </jats:italic> oxidase and photosystem) in both Δ <jats:italic>copI</jats:italic> and <jats:italic>copA</jats:italic> -null mutants, but the causes are different. In the <jats:italic>copA</jats:italic> mutant, heme and chlorophyll synthesis are affected, whereas in Δ <jats:italic>copI</jats:italic> mutant, the decrease is a consequence of impaired cytochrome <jats:italic>c</jats:italic> assembly. This impact on <jats:italic>c</jats:italic> -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. </jats:p> <jats:p> <jats:bold>IMPORTANCE</jats:bold> Copper is an essential cation required as a cofactor in enzymes involved in vital processes such as respiration, photosynthesis, free radical scavenging, and pathogenesis. However, copper is highly toxic and has been implicated in disorders in all organisms, including humans, because it can catalyze the production of toxic reactive oxygen species and targets various biosynthesis pathways. Identifying copper targets, provides insights into copper toxicity and homeostatic mechanisms for copper tolerance. In this work, we describe for the first time a direct effect of excess copper on cytochrome <jats:italic>c</jats:italic> assembly. We show that excess copper specifically affects periplasmic and membrane cytochromes <jats:italic>c</jats:italic> , thus suggesting that the copper toxicity targets <jats:italic>c</jats:italic> -type cytochrome biogenesis. </jats:p>

収録刊行物

  • mBio

    mBio 6 (5), 2015-10-30

    American Society for Microbiology

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