Evidence map›Paper›PMID 21498632›Full record

ArticleJournal of experimental botany2011

Inter-species variation in the oligomeric states of the higher plant Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase.

Thomas P Howard, Julie C Lloyd, Christine A Raines

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Journal of experimental botany, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 'Autophagy · 2023
    Article
  6. NTRC regulates CP12 to activate Calvin-Benson cycle during cold acclimation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Reduction in Phosphoribulokinase Amount and Re-Routing Metabolism inInternational journal of molecular sciences · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Review
  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

3 authors at 1 institution in 1 country.

Thomas P HowardDepartment of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK. T.P.Howard@exeter.ac.uk
Julie C Lloyd
Christine A Raines
University of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BBSRC P19403Biotechnology and Biological Sciences Research Council P19403
6 · The paper itself

Abstract

In darkened leaves the Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) form a regulatory multi-enzyme complex with the small chloroplast protein CP12. GAPDH also forms a high molecular weight regulatory mono-enzyme complex. Given that there are different reports as to the number and subunit composition of these complexes and that enzyme regulatory mechanisms are known to vary between species, it was reasoned that protein-protein interactions may also vary between species. Here, this variation is investigated. This study shows that two different tetramers of GAPDH (an A2B2 heterotetramer and an A4 homotetramer) have the capacity to form part of the PRK/GAPDH/CP12 complex. The role of the PRK/GAPDH/CP12 complex is not simply to regulate the 'non-regulatory' A4 GAPDH tetramer. This study also demonstrates that the abundance and nature of PRK/GAPDH/CP12 interactions are not equal in all species and that whilst NAD enhances complex formation in some species, this is not sufficient for complex formation in others. Furthermore, it is shown that the GAPDH mono-enzyme complex is more abundant as a 2(A2B2) complex, rather than the larger 4(A2B2) complex. This smaller complex is sensitive to cellular metabolites indicating that it is an important regulatory isoform of GAPDH. This comparative study has highlighted considerable heterogeneity in PRK and GAPDH protein interactions between closely related species and the possible underlying physiological basis for this is discussed.

Indexed as

ChloroplastsGlyceraldehyde-3-Phosphate DehydrogenasesNADPhosphotransferases (Alcohol Group Acceptor)PhotosynthesisPlant ProteinsPlantsProtein IsoformsSpecies SpecificityGlyceraldehyde-3-Phosphate DehydrogenasesNADphosphoribulokinasePhosphotransferases (Alcohol Group Acceptor)Plant ProteinsProtein Isoforms

Identifiers

PMID21498632
PMCPMC3134340
OpenAlexW2125128804

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.