Evidence map›Paper›PMID 31504763›Full record

ArticleJournal of experimental botany2019

The pyrenoidal linker protein EPYC1 phase separates with hybrid Arabidopsis-Chlamydomonas Rubisco through interactions with the algal Rubisco small subunit.

Nicky Atkinson, Christos N Velanis, Tobias Wunder, David J Clarke, Oliver Mueller-Cajar, Alistair J McCormick

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.8field-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

29 citing papers in PubMed, 64 citations in OpenAlex.

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  14. Pyrenoid proteomics reveals independent evolution of the COProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. SAGA1 and SAGA2 promote starch formation around proto-pyrenoids in Arabidopsis chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Nicky AtkinsonSynthSys and Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Christos N VelanisSynthSys and Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Tobias WunderSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
David J ClarkeSchool of Chemistry, University of Edinburgh, Edinburgh, UK.
Oliver Mueller-CajarSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Alistair J McCormickSynthSys and Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, UK.
University of Edinburgh · GBNanyang Technological University · SG

Funding

Biotechnology and Biological Sciences Research Council BB/M006468/1Wellcome Trust WT104915MA
6 · The paper itself

Abstract

Photosynthetic efficiencies in plants are restricted by the CO2-fixing enzyme Rubisco but could be enhanced by introducing a CO2-concentrating mechanism (CCM) from green algae, such as Chlamydomonas reinhardtii (hereafter Chlamydomonas). A key feature of the algal CCM is aggregation of Rubisco in the pyrenoid, a liquid-like organelle in the chloroplast. Here we have used a yeast two-hybrid system and higher plants to investigate the protein-protein interaction between Rubisco and essential pyrenoid component 1 (EPYC1), a linker protein required for Rubisco aggregation. We showed that EPYC1 interacts with the small subunit of Rubisco (SSU) from Chlamydomonas and that EPYC1 has at least five SSU interaction sites. Interaction is crucially dependent on the two surface-exposed α-helices of the Chlamydomonas SSU. EPYC1 could be localized to the chloroplast in higher plants and was not detrimental to growth when expressed stably in Arabidopsis with or without a Chlamydomonas SSU. Although EPYC1 interacted with Rubisco in planta, EPYC1 was a target for proteolytic degradation. Plants expressing EPYC1 did not show obvious evidence of Rubisco aggregation. Nevertheless, hybrid Arabidopsis Rubisco containing the Chlamydomonas SSU could phase separate into liquid droplets with purified EPYC1 in vitro, providing the first evidence of pyrenoid-like aggregation for Rubisco derived from a higher plant.

Indexed as

Algal ProteinsArabidopsisChlamydomonas reinhardtiiPlants, Genetically ModifiedRibulose-Bisphosphate CarboxylaseAlgal ProteinsRibulose-Bisphosphate CarboxylaseArabidopsis thalianaChlamydomonas reinhardtiichloroplastCO2-concentrating mechanismNicotiana benthamianaphotosynthesispyrenoid

Identifiers

PMID31504763
PMCPMC6793452
OpenAlexW2969789283

What OpenQuestion holds

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LicenceCC BY-NC
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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.