Evidence map›Paper›PMID 38591346›Full record

ArticlePlant & cell physiology2024

APX2 Is an Ascorbate Peroxidase-Related Protein that Regulates the Levels of Plastocyanin in Chlamydomonas.

Anna Caccamo, Félix Vega de Luna, Agnieszka E Misztak, Sébastien Pyr Dit Ruys, Didier Vertommen, Pierre Cardol, Joris Messens, Claire Remacle

Abstract read
In one paragraph

Article in Plant & cell physiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
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

8 authors.

Anna CaccamoGenetics and Physiology of Microalgae, InBios/Phytosystems Research Unit, University of Liège, Chemin de la vallée 4, Liège 4000, Belgium.ORCID 0000-0002-3147-313X
Félix Vega de LunaGenetics and Physiology of Microalgae, InBios/Phytosystems Research Unit, University of Liège, Chemin de la vallée 4, Liège 4000, Belgium.ORCID 0000-0003-3935-7499
Agnieszka E MisztakGenetics and Physiology of Microalgae, InBios/Phytosystems Research Unit, University of Liège, Chemin de la vallée 4, Liège 4000, Belgium.ORCID 0000-0001-5977-3532
Sébastien Pyr Dit Ruysde Duve Institute and MASSPROT platform, UCLouvain, Avenue Hippocrate 74, Brussels 1200, Belgium.ORCID 0000-0002-5449-1541
Didier Vertommende Duve Institute and MASSPROT platform, UCLouvain, Avenue Hippocrate 74, Brussels 1200, Belgium.ORCID 0000-0001-7648-8282
Pierre CardolGenetics and Physiology of Microalgae, InBios/Phytosystems Research Unit, University of Liège, Chemin de la vallée 4, Liège 4000, Belgium.ORCID 0000-0001-9799-0546
Joris MessensVIB-VUB Center for Structural Biology, Pleinlaan 2, Brussels 1050, Belgium.ORCID 0000-0002-2128-8264
Claire RemacleGenetics and Physiology of Microalgae, InBios/Phytosystems Research Unit, University of Liège, Chemin de la vallée 4, Liège 4000, Belgium.ORCID 0000-0002-5016-9547

Funding

Fonds de la Recherche Scientifique -FNRS 33663953Research Foundation Flanders-Fonds de la Recherche Scientifique Excellence of Science project no.30829584VIB grant
6 · The paper itself

Abstract

The function of ascorbate peroxidase-related (APX-R) proteins, present in all green photosynthetic eukaryotes, remains unclear. This study focuses on APX-R from Chlamydomonas reinhardtii, namely, ascorbate peroxidase 2 (APX2). We showed that apx2 mutants exhibited a faster oxidation of the photosystem I primary electron donor, P700, upon sudden light increase and a slower re-reduction rate compared to the wild type, pointing to a limitation of plastocyanin. Spectroscopic, proteomic and immunoblot analyses confirmed that the phenotype was a result of lower levels of plastocyanin in the apx2 mutants. The redox state of P700 did not differ between wild type and apx2 mutants when the loss of function in plastocyanin was nutritionally complemented by growing apx2 mutants under copper deficiency. In this case, cytochrome c6 functionally replaces plastocyanin, confirming that lower levels of plastocyanin were the primary defect caused by the absence of APX2. Overall, the results presented here shed light on an unexpected regulation of plastocyanin level under copper-replete conditions, induced by APX2 in Chlamydomonas.

Indexed as

Ascorbate PeroxidasesChlamydomonas reinhardtiiMutationPlastocyaninCopperCytochromes c6LightOxidation-ReductionPhotosystem I Protein ComplexPlant ProteinsProteomicsAscorbate PeroxidasesCopperCytochromes c6Photosystem I Protein ComplexPlant ProteinsPlastocyaninAPX2ChlamydomonasCopper deficiencyCytochrome c6P700Plastocyanin

Identifiers

PMID38591346
PMCPMC11094752

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Registered trials

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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.