Evidence map›Paper›PMID 30815863›Full record

ArticleFEBS letters2019

Improved recombinant expression and purification of functional plant Rubisco.

Robert H Wilson, Gabriel Thieulin-Pardo, Franz-Ulrich Hartl, Manajit Hayer-Hartl

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Rubisco kinetic acclimation at the holoenzyme level.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. A temporal gradient of cytonuclear coordination of chaperonins and chaperones during RuBisCo biogenesis in allopolyploid plants.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Elucidation and genetic intervention of COJournal of biosciences · 2020
    Article
  18. 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 2 institutions in 1 country.

Robert H WilsonChaperonin-assisted Protein Folding Group, Max Planck Institute of Biochemistry, Martinsried, Germany.
Gabriel Thieulin-PardoChaperonin-assisted Protein Folding Group, Max Planck Institute of Biochemistry, Martinsried, Germany.
Franz-Ulrich HartlCellular Biochemistry Group, Max Planck Institute of Biochemistry, Martinsried, Germany.
Manajit Hayer-HartlChaperonin-assisted Protein Folding Group, Max Planck Institute of Biochemistry, Martinsried, Germany.
Max Planck Institute of Biochemistry · DEMax Planck Research Unit for Enzymology of Protein Folding · DE

Funding

Deutsche Forschungsgemeinschaft (DFG) SFB1035Minerva Foundation of the Max Planck Society
6 · The paper itself

Abstract

Improving the performance of the key photosynthetic enzyme Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) by protein engineering is a critical strategy for increasing crop yields. The extensive chaperone requirement of plant Rubisco for folding and assembly has long been an impediment to this goal. Production of plant Rubisco in Escherichia coli requires the coexpression of the chloroplast chaperonin and four assembly factors. Here, we demonstrate that simultaneous expression of Rubisco and chaperones from a T7 promotor produces high levels of functional enzyme. Expressing the small subunit of Rubisco with a C-terminal hexahistidine-tag further improved assembly, resulting in a ~ 12-fold higher yield than the previously published procedure. The expression system described here provides a platform for the efficient production and engineering of plant Rubisco.

Indexed as

ArabidopsisArabidopsis ProteinsCarbon DioxideCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsGroup I ChaperoninsHistidineKineticsModels, MolecularMolecular ChaperonesOligopeptidesPhosphate-Binding ProteinsPhotosynthesisProtein FoldingArabidopsis ProteinsAT1G26230 protein, ArabidopsisCarbon DioxideCpn20 protein, ArabidopsisGroup I ChaperoninsHis-His-His-His-His-HisHistidineMolecular ChaperonesOligopeptidesPhosphate-Binding ProteinsProtein IsoformsProtein SubunitsRAF1 protein, ArabidopsisRbcX2 protein, ArabidopsisRecombinant Fusion ProteinsRibulose-Bisphosphate Carboxylaseassemblyfoldingmolecular chaperonesprotein expressionRubiscoRubisco activase

Identifiers

PMID30815863
PMCPMC6593764
OpenAlexW2919022368

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.