Evidence map›Paper›PMID 16126858›Full record

ArticlePlant physiology2005

A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis.

Chiung-Chih Chu, Wen-Chi Lee, Wen-Yu Guo, Shu-Mei Pan, Lih-Jen Chen, Hsou-Min Li, Tsung-Luo Jinn

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

74 citing papers in PubMed, 183 citations in OpenAlex.

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  13. Article
  14. Article
  15. Physiological and Molecular Mechanisms of Plant Responses to Copper Stress.International journal of molecular sciences · 2022
    Review
  16. MicroRNA398: A Master Regulator of Plant Development and Stress Responses.International journal of molecular sciences · 2022
    Review
  17. Article
  18. Article
  19. Review
  20. Article

14 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Chiung-Chih ChuDepartment of Life Science and Institute of Plant Biology, National Taiwan University, Taipei.
Wen-Chi Lee
Wen-Yu Guo
Shu-Mei Pan
Lih-Jen Chen
Hsou-Min Li
Tsung-Luo Jinn
Institute of Molecular Biology, Academia Sinica · TWNational Taiwan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The copper chaperone for superoxide dismutase (CCS) has been identified as a key factor integrating copper into copper/zinc superoxide dismutase (CuZnSOD) in yeast (Saccharomyces cerevisiae) and mammals. In Arabidopsis (Arabidopsis thaliana), only one putative CCS gene (AtCCS, At1g12520) has been identified. The predicted AtCCS polypeptide contains three distinct domains: a central domain, flanked by an ATX1-like domain, and a C-terminal domain. The ATX1-like and C-terminal domains contain putative copper-binding motifs. We have investigated the function of this putative AtCCS gene and shown that a cDNA encoding the open reading frame predicted by The Arabidopsis Information Resource complemented only the cytosolic and peroxisomal CuZnSOD activities in the Atccs knockout mutant, which has lost all CuZnSOD activities. However, a longer AtCCS cDNA, as predicted by the Munich Information Centre for Protein Sequences and encoding an extra 66 amino acids at the N terminus, could restore all three, including the chloroplastic CuZnSOD activities in the Atccs mutant. The extra 66 amino acids were shown to direct the import of AtCCS into chloroplasts. Our results indicated that one AtCCS gene was responsible for the activation of all three types of CuZnSOD activity. In addition, a truncated AtCCS, containing only the central and C-terminal domains without the ATX1-like domain failed to restore any CuZnSOD activity in the Atccs mutant. This result indicates that the ATX1-like domain is essential for the copper chaperone function of AtCCS in planta.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsCopperGene DeletionGene Expression Regulation, PlantGenetic Complementation TestMolecular ChaperonesMolecular Sequence DataPlant LeavesPlants, Genetically ModifiedProtein Structure, TertiarySequence Homology, Amino AcidSuperoxide DismutaseZincArabidopsis ProteinsCCS protein, ArabidopsisCopperMolecular ChaperonesSuperoxide DismutaseZinc

Identifiers

PMID16126858
PMCPMC1203391
OpenAlexW2165707168

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.