The Copper Metallome in Prokaryotic Cells

Rensing, Christopher; Alwathnani, Hend A.; McDevitt, Sylvia Franke

doi:10.1002/9781119004813.ch13

Cited by 9 publications

(10 citation statements)

References 145 publications

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“…2,16 These CopCs could also donate Cu(II) to other proteins in the periplasm, including Cop proteins. In this scenario, the C 1−1 CopCs would function similarly and may also participate in Cu(I) detoxification.…”

Section: Resultsmentioning

confidence: 99%

“…1,2 It is a critical cofactor in proteins such as cytochrome c oxidase, superoxide dismutase, and numerous oxygenases, but excess copper causes oxidative damage and may disrupt iron–sulfur clusters. 1–4 To satisfy intracellular copper requirements and avoid toxicity, bacteria have evolved multiple copper homeostasis pathways.…”

mentioning

confidence: 99%

“…It has been suggested that the Cop proteins export copper, 9 import copper to the cytoplasm, 2,16 and/or sequester copper in the periplasm. 17,18 The possibility of import has been relatively underinvestigated, likely due to the fact that there is no known function for copper in the bacterial cytoplasm beyond its involvement in copper homeostasis and gene regulation.…”

mentioning

confidence: 99%

“…17,18 The possibility of import has been relatively underinvestigated, likely due to the fact that there is no known function for copper in the bacterial cytoplasm beyond its involvement in copper homeostasis and gene regulation. 2 The traditional Cop/Pco system is composed of seven proteins, CopABCDERS. CopD and CopB are inner and outer membrane proteins, respectively (CopB should not be confused with the identically named copper-transporting P 1B -type ATPase, not traditionally part of the cop operon).…”

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confidence: 99%

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The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

et al. 2016

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The CopC proteins are periplasmic copper binding proteins believed to play a role in bacterial copper homeostasis. Previous studies have focused on CopCs that are part of seven-protein Cop or Pco systems involved in copper resistance. These canonical CopCs contain distinct Cu(I) and Cu(II) binding sites. Mounting evidence suggests that CopCs are more widely distributed, often present only with the CopD inner membrane protein, frequently as a fusion protein, and that the CopC and CopD proteins together function in the uptake of copper to the cytoplasm. In the methanotroph Methylosinus trichosporium OB3b, genes encoding a CopCD pair are located adjacent to the particulate methane monooxygenase (pMMO) operon. The CopC from this organism (Mst-CopC) was expressed, purified, and structurally characterized. The 1.46 Å resolution crystal structure of Mst-CopC reveals a single Cu(II) binding site with coordination somewhat different from that in canonical CopCs, and the absence of a Cu(I) binding site. Extensive bioinformatic analyses indicate that the majority of CopCs in fact contain only a Cu(II) site, with just 10% of sequences corresponding to the canonical two-site CopC. Accordingly, a new classification scheme for CopCs was developed, and detailed analyses of the sequences and their genomic neighborhoods reveal new proteins potentially involved in copper homeostasis, providing a framework for expanded models of CopCD function.

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Section: Resultsmentioning

confidence: 99%

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The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

et al. 2016

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“…Copper (Cu) is an essential but potentially toxic micro-nutrient that serves as a cofactor for important enzymes, like cytochrome oxidases (Cox) or multicopper oxidases (laccases) (Ekici et al, 2012a;Rensing and McDevitt, 2013). Cu is a strong soft metal that can attack intracellular iron-sulfur centers of various proteins primarily under anoxic conditions (Macomber and Imlay, 2009).…”

Section: Introductionmentioning

confidence: 99%

The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb₃ oxidase assembly

Utz

Andrei

Milanov

et al. 2019

Molecular Microbiology

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Summary Cu homeostasis depends on a tightly regulated network of proteins that transport or sequester Cu, preventing the accumulation of this toxic metal while sustaining Cu supply for cuproproteins. In Rhodobacter capsulatus, Cu‐detoxification and Cu delivery for cytochrome c oxidase (cbb3‐Cox) assembly depend on two distinct Cu‐exporting P1B‐type ATPases. The low‐affinity CopA is suggested to export excess Cu and the high‐affinity CcoI feeds Cu into a periplasmic Cu relay system required for cbb3‐Cox biogenesis. In most organisms, CopA‐like ATPases receive Cu for export from small Cu chaperones like CopZ. However, whether these chaperones are also involved in Cu export via CcoI‐like ATPases is unknown. Here we identified a CopZ‐like chaperone in R. capsulatus, determined its cellular concentration and its Cu binding activity. Our data demonstrate that CopZ has a strong propensity to form redox‐sensitive dimers via two conserved cysteine residues. A ΔcopZ strain, like a ΔcopA strain, is Cu‐sensitive and accumulates intracellular Cu. In the absence of CopZ, cbb3‐Cox activity is reduced, suggesting that CopZ not only supplies Cu to P1B‐type ATPases for detoxification but also for cuproprotein assembly via CcoI. This finding was further supported by the identification of a ~150 kDa CcoI‐CopZ protein complex in native R. capsulatus membranes.

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Copper (II) Ion Action on Soil Bacteria

Asatiani

Abuladze

Kartvelishvili

et al. 2021

Water Air Soil Pollut

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The Copper Metallome in Prokaryotic Cells

Cited by 9 publications

References 145 publications

The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb₃ oxidase assembly

Copper (II) Ion Action on Soil Bacteria

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The Copper Metallome in Prokaryotic Cells

Cited by 9 publications

References 145 publications

The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb3 oxidase assembly

Copper (II) Ion Action on Soil Bacteria

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The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb₃ oxidase assembly