Evidence map›Paper›PMID 26237510›Full record

ArticleNature structural & molecular biology2015

Structure and mechanism of the Rubisco-assembly chaperone Raf1.

Thomas Hauser, Javaid Y Bhat, Goran Miličić, Petra Wendler, F Ulrich Hartl, Andreas Bracher, Manajit Hayer-Hartl

Abstract read
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Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. 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
  8. Article
  9. Engineering COPlant communications · 2025
    Article
  10. Article
  11. Review
  12. Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024
    Review
  13. Article
  14. Article
  15. 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
  16. Overexpression ofGenes · 2022
    Article
  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

7 authors.

Thomas HauserDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Javaid Y BhatDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Goran MiličićDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Petra WendlerGene Center Munich, Ludwig-Maximilians-Universität München, Munich, Germany.
F Ulrich HartlDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Andreas BracherDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0001-8530-7594
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

Biogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of ∼40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL8 complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a β-sheet dimerization domain and a flexibly linked α-helical domain. Chemical cross-linking and EM reconstruction indicate that the β-domains bind along the equator of each RbcL2 unit, and the α-helical domains embrace the top and bottom edges of RbcL2. Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis.

Indexed as

ArabidopsisArabidopsis ProteinsCrystallography, X-RayModels, MolecularMolecular WeightProtein ConformationProtein MultimerizationSynechococcusArabidopsis ProteinsRAF1 protein, Arabidopsis

Identifiers

PMID26237510

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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.