Evidence map›Paper›PMID 26718481›Full record

ArticleMolecular microbiology2016

Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus.

Petru-Iulian Trasnea, Marcel Utz, Bahia Khalfaoui-Hassani, Simon Lagies, Fevzi Daldal, Hans-Georg Koch

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. AccA fromChemical science · 2026
    Article
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  5. Review
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  8. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. The CopA2-Type PFrontiers in microbiology · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. PCuThe Journal of biological chemistry · 2019
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Petru-Iulian TrasneaInstitut für Biochemie und Molekularbiologie, ZBMZ, Stefan-Meier-Strasse 17, 79104, Freiburg, Germany.
Marcel UtzInstitut für Biochemie und Molekularbiologie, ZBMZ, Stefan-Meier-Strasse 17, 79104, Freiburg, Germany.
Bahia Khalfaoui-HassaniDepartment of Biology, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Simon LagiesInstitut für Biochemie und Molekularbiologie, ZBMZ, Stefan-Meier-Strasse 17, 79104, Freiburg, Germany.
Fevzi DaldalDepartment of Biology, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Hans-Georg KochInstitut für Biochemie und Molekularbiologie, ZBMZ, Stefan-Meier-Strasse 17, 79104, Freiburg, Germany.
University of Pennsylvania · USUniversity of Freiburg · DE

Funding

Respiratory Complex III: Supercomplexes and ROS, from Bacteria to HumanR01GM038237 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DALDAL, M. FEVZI · 1987 to 2018
$5.9M
NIGMS NIH HHS GM38237NIGMS NIH HHS R01 GM038237
6 · The paper itself

Abstract

Copper (Cu) is an essential micronutrient that functions as a cofactor in several important enzymes, such as respiratory heme-copper oxygen reductases. Yet, Cu is also toxic and therefore cells engage a highly coordinated Cu uptake and delivery system to prevent the accumulation of toxic Cu concentrations. In this study, we analyzed Cu delivery to the cbb3 -type cytochrome c oxidase (cbb3 -Cox) of Rhodobacter capsulatus. We identified the PCuA C-like periplasmic chaperone PccA and analyzed its contribution to cbb3 -Cox assembly. Our data demonstrate that PccA is a Cu-binding protein with a preference for Cu(I), which is required for efficient cbb3 -Cox assembly, in particular, at low Cu concentrations. By using in vivo and in vitro cross-linking, we show that PccA forms a complex with the Sco1-homologue SenC. This complex is stabilized in the absence of the cbb3 -Cox-specific assembly factors CcoGHIS. In cells lacking SenC, the cytoplasmic Cu content is significantly increased, but the simultaneous absence of PccA prevents this Cu accumulation. These data demonstrate that the interplay between PccA and SenC not only is required for Cu delivery during cbb3 -Cox assembly but also regulates Cu homeostasis in R. capsulatus.

Indexed as

Bacterial ProteinsCopperCytoplasmElectron Transport Complex IVHemeHomeostasisMetallochaperonesOxidation-ReductionOxidoreductasesPeriplasmRhodobacter capsulatusBacterial Proteinscbb3 oxidaseCopperElectron Transport Complex IVHemeMetallochaperonesOxidoreductases

Identifiers

PMID26718481
PMCPMC4878679
OpenAlexW2219424245

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.