Evidence map›Paper›PMID 25558973›Full record

ArticleNature chemical biology2015

Opposing effects of folding and assembly chaperones on evolvability of Rubisco.

Paulo Durão, Harald Aigner, Péter Nagy, Oliver Mueller-Cajar, F Ulrich Hartl, Manajit Hayer-Hartl

Abstract read
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Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Directed evolution of a plant Rubisco chaperone with altered client recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. In vivo directed evolution of an ultrafast Rubisco from a semianaerobic environment imparts oxygen resistance.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
  11. Review
  12. Rubisco is evolving for improved catalytic efficiency and COProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

6 authors.

Paulo DurãoDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Harald AignerDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Péter NagyDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Oliver Mueller-CajarDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
F Ulrich HartlDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Manajit Hayer-HartlDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the fixation of CO2 in photosynthesis. Despite its pivotal role, Rubisco is an inefficient enzyme and thus is a key target for directed evolution. Rubisco biogenesis depends on auxiliary factors, including the GroEL/ES-type chaperonin for folding and the chaperone RbcX for assembly. Here we performed directed evolution of cyanobacterial form I Rubisco using a Rubisco-dependent Escherichia coli strain. Overexpression of GroEL/ES enhanced Rubisco solubility and tended to expand the range of permissible mutations. In contrast, the specific assembly chaperone RbcX had a negative effect on evolvability by preventing a subset of mutants from forming holoenzyme. Mutation F140I in the large Rubisco subunit, isolated in the absence of RbcX, increased carboxylation efficiency approximately threefold without reducing CO2 specificity. The F140I mutant resulted in a ∼55% improved photosynthesis rate in Synechocystis PCC6803. The requirement of specific biogenesis factors downstream of chaperonin may have retarded the natural evolution of Rubisco.

Indexed as

Protein FoldingProtein MultimerizationBacterial ProteinsDirected Molecular EvolutionEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsMolecular ChaperonesMutationPhotosynthesisRibulose-Bisphosphate CarboxylaseSynechococcusSynechocystisBacterial ProteinsEscherichia coli ProteinsGroE protein, E coliHeat-Shock ProteinsMolecular ChaperonesRbcX protein, cyanobacteriaRibulose-Bisphosphate Carboxylase

Identifiers

PMID25558973

What OpenQuestion holds

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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.