Evidence map›Paper›PMID 32451445›Full record

ArticleNature plants2020

Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1.

Ling-Yun Xia, Yong-Liang Jiang, Wen-Wen Kong, Hui Sun, Wei-Fang Li, Yuxing Chen, Cong-Zhao Zhou

Abstract read
PubMed Publisher
In one paragraph

Article in Nature plants, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. 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
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Towards engineering a hybrid carboxysome.Photosynthesis research · 2023
    Article
  17. Article
  18. Review
  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 at 1 institution in 1 country.

Ling-Yun Xia *Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China.ORCID http://orcid.org/0000-0001-6329-9650
Yong-Liang Jiang *Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China. jyl@ustc.edu.cn.ORCID http://orcid.org/0000-0001-5441-4936
Wen-Wen Kong *Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China.ORCID http://orcid.org/0000-0001-6955-3517
Hui SunHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China.ORCID http://orcid.org/0000-0003-2248-5363
Wei-Fang LiHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China.ORCID http://orcid.org/0000-0002-2653-0785
Yuxing ChenHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China. cyxing@ustc.edu.cn.ORCID http://orcid.org/0000-0002-7560-1922
Cong-Zhao ZhouHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, China. zcz@ustc.edu.cn.ORCID http://orcid.org/0000-0002-6881-7151
University of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The folding and assembly of RuBisCO, the most abundant enzyme in nature, needs a series of chaperones, including the RuBisCO accumulation factor Raf1, which is highly conserved in cyanobacteria and plants. Here, we report the crystal structures of Raf1 from cyanobacteria Anabaena sp. PCC 7120 and its complex with RuBisCO large subunit RbcL. Structural analyses and biochemical assays reveal that each Raf1 dimer captures an RbcL dimer, with the C-terminal tail inserting into the catalytic pocket, and further mediates the assembly of RbcL dimers to form the octameric core of RuBisCO. Furthermore, the cryo-electron microscopy structures of the RbcL-Raf1-RbcS assembly intermediates enable us to see a dynamic assembly process from RbcL

Indexed as

Amino Acid SequenceAnabaenaBacterial ProteinsMolecular ChaperonesPlant ProteinsProtein Structure, SecondaryRibulose-Bisphosphate CarboxylaseSequence AlignmentBacterial ProteinsMolecular ChaperonesPlant ProteinsRibulose-Bisphosphate Carboxylase

Identifiers

PMID32451445
OpenAlexW3027134327

What OpenQuestion holds

Textmetadata
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.