Evidence map›Paper›PMID 21878617›Full record

ArticleThe Journal of biological chemistry2011

Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope Cu(I)-ATPase.

Patrice Catty, Sylvain Boutigny, Roger Miras, Jacques Joyard, Norbert Rolland, Daphné Seigneurin-Berny

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In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.6field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  5. Article
  6. Ectopic Expression ofInternational journal of molecular sciences · 2023
    Article
  7. Physiological and Molecular Mechanisms of Plant Responses to Copper Stress.International journal of molecular sciences · 2022
    Review
  8. Biomolecules · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. 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 5 institutions in 1 country.

Patrice CattyLaboratoire de Chimie et Biologie des Métaux, UMR5249, CNRS, F-38054 Grenoble, France.
Sylvain Boutigny
Roger Miras
Jacques Joyard
Norbert Rolland
Daphné Seigneurin-Berny
Institut de Recherches en Technologies et Sciences pour le Vivant · FRCEA Grenoble · FRCentre National de la Recherche Scientifique · FRLaboratoire de Physiologie CellulaireLaboratoire Physiologie Cellulaire & Végétale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Copper is an essential plant micronutrient playing key roles in cellular processes, among them photosynthesis. In Arabidopsis thaliana, copper delivery to chloroplasts, mainly studied by genetic approaches, is thought to involve two P(IB)-type ATPases: AtHMA1 and AtHMA6/PAA1. The lack of biochemical characterization of AtHMA1 and PAA1, and more generally of plant P(IB)-type ATPases, is due to the difficulty of getting high amounts of these membrane proteins in an active form, either from their native environment or after expression in heterologous systems. In this study, we report the first biochemical characterization of PAA1, a plant copper-transporting ATPase. PAA1 produced in Lactococcus lactis is active, forming an aspartyl phosphate intermediate in the presence of ATP and the adequate metal ion. PAA1 can also be phosphorylated using inorganic phosphate in the absence of transition metal. Both phosphorylation types allowed us to demonstrate that PAA1 is activated by monovalent copper ions (and to a lower extent by silver ions) with an apparent affinity in the micromolar range. In agreement with these biochemical data, we also demonstrate that when expressed in yeast, PAA1 induces increased sensitivities to copper and silver. These data provide the first enzymatic characterization of a P(IB-1)-type plant ATPase and clearly identify PAA1 as a high affinity Cu(I) transporter of the chloroplast envelope.

Indexed as

ArabidopsisArabidopsis ProteinsCations, MonovalentChloroplast Proton-Translocating ATPasesChloroplastsCopperIon TransportLactococcus lactisArabidopsis ProteinsCations, MonovalentChloroplast Proton-Translocating ATPasesCopperPAA1 protein, Arabidopsis

Identifiers

PMID21878617
PMCPMC3196147
OpenAlexW1967395613

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.