Evidence map›Paper›PMID 25371207›Full record

ArticleThe Journal of biological chemistry2015

Role of small subunit in mediating assembly of red-type form I Rubisco.

Jidnyasa Joshi, Oliver Mueller-Cajar, Yi-Chin C Tsai, F Ulrich Hartl, Manajit Hayer-Hartl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. 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
1.7field-weighted citation impact, top 16% 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, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Rubisco is evolving for improved catalytic efficiency and COProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. The dependency of red Rubisco on its cognate activase for enhancing plant photosynthesis and growth.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Elevated COBMC plant biology · 2019
    Article
  15. Article
  16. Article
  17. Metabolic engineering communications · 2017
    Article
  18. Review
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

5 authors at 1 institution in 1 country.

Jidnyasa JoshiFrom the Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Oliver Mueller-CajarFrom the Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Yi-Chin C TsaiFrom the Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
F Ulrich HartlFrom the Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Manajit Hayer-HartlFrom the Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany mhartl@biochem.mpg.de.
Max Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in photosynthetic carbon fixation, converting atmospheric CO2 to organic compounds. Form I Rubisco is a cylindrical complex composed of eight large (RbcL) subunits that are capped by four small subunits (RbcS) at the top and four at the bottom. Form I Rubiscos are phylogenetically divided into green- and red-type. Some red-type enzymes have catalytically superior properties. Thus, understanding their folding and assembly is of considerable biotechnological interest. Folding of the green-type RbcL subunits in cyanobacteria is mediated by the GroEL/ES chaperonin system, and assembly to holoenzyme requires specialized chaperones such as RbcX and RAF1. Here, we show that the red-type RbcL subunits in the proteobacterium Rhodobacter sphaeroides also fold with GroEL/ES. However, assembly proceeds in a chaperone-independent manner. We find that the C-terminal β-hairpin extension of red-type RbcS, which is absent in green-type RbcS, is critical for efficient assembly. The β-hairpins of four RbcS subunits form an eight-stranded β-barrel that protrudes into the central solvent channel of the RbcL core complex. The two β-barrels stabilize the complex through multiple interactions with the RbcL subunits. A chimeric green-type RbcS carrying the C-terminal β-hairpin renders the assembly of a cyanobacterial Rubisco independent of RbcX. Our results may facilitate the engineering of crop plants with improved growth properties expressing red-type Rubisco.

Indexed as

Bacterial ProteinsChaperonin 60Molecular ChaperonesPhotosynthesisProtein FoldingProto-Oncogene Proteins c-rafRhodobacter sphaeroidesRibulose-Bisphosphate CarboxylaseRibulosephosphatesBacterial ProteinsChaperonin 60Molecular ChaperonesProto-Oncogene Proteins c-rafRbcX protein, cyanobacteriaribulose-1,5 diphosphateRibulose-Bisphosphate CarboxylaseRibulosephosphatesMolecular ChaperonePhotosynthesisProtein AssemblyProtein FoldingRibulose-1,5-bisphosphate Carboxylase/Oxygenase (RuBisCO)

Identifiers

PMID25371207
PMCPMC4294474
OpenAlexW2055115467

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.