Evidence map›Paper›PMID 33625514›Full record

ArticleThe Plant cell2021

The state of oligomerization of Rubisco controls the rate of synthesis of the Rubisco large subunit in Chlamydomonas reinhardtii.

Wojciech Wietrzynski, Eleonora Traverso, Francis-André Wollman, Katia Wostrikoff

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Transfer of chloroplastSynthetic and systems biotechnology · 2027
    Article
  2. Rewinding evolution in planta: A Rubisco-null platform validates high-performance ancestral enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. The chloroplast RNA-binding protein CP29A supportsProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024
    Review
  10. Article
  11. Article
  12. Plant organellar RNA maturation.The Plant cell · 2023
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
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

4 authors at 1 institution in 2 countries.

Wojciech WietrzynskiSorbonne Université, CNRS, Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, 75005 Paris, France.ORCID 0000-0001-8898-2392
Eleonora TraversoSorbonne Université, CNRS, Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, 75005 Paris, France.ORCID 0000-0001-9019-0378
Francis-André WollmanSorbonne Université, CNRS, Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, 75005 Paris, France.ORCID 0000-0003-2638-7840
Katia WostrikoffSorbonne Université, CNRS, Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, 75005 Paris, France.ORCID 0000-0002-5358-9117
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is present in all photosynthetic organisms and is a key enzyme for photosynthesis-driven life on Earth. Its most prominent form is a hetero-oligomer in which small subunits (SSU) stabilize the core of the enzyme built from large subunits (LSU), yielding, after a chaperone-assisted multistep assembly process, an LSU8SSU8 hexadecameric holoenzyme. Here we use Chlamydomonas reinhardtii and a combination of site-directed mutants to dissect the multistep biogenesis pathway of Rubisco in vivo. We identify assembly intermediates, in two of which LSU are associated with the RAF1 chaperone. Using genetic and biochemical approaches we further unravel a major regulation process during Rubisco biogenesis, in which LSU translation is controlled by its ability to assemble with the SSU, via the mechanism of control by epistasy of synthesis (CES). Altogether this leads us to propose a model whereby the last assembly intermediate, an LSU8-RAF1 complex, provides the platform for SSU binding to form the Rubisco enzyme, and when SSU is not available, converts to a key regulatory form that exerts negative feedback on the initiation of LSU translation.

Indexed as

Protein BiosynthesisProtein Multimerization5' Untranslated RegionsChlamydomonas reinhardtiiDown-RegulationModels, BiologicalMutationProtein BindingProtein StabilityProtein SubunitsRibulose-Bisphosphate Carboxylase5' Untranslated RegionsProtein SubunitsRibulose-Bisphosphate Carboxylase

Identifiers

PMID33625514
PMCPMC8254502
OpenAlexW3131597813

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.