Evidence map›Paper›PMID 20304968›Full record

ArticlePlant physiology2010

Functional cyanobacterial beta-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein.

Benedict M Long, Loraine Tucker, Murray R Badger, G Dean Price

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.2field-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

63 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026
    Review
  5. Article
  6. Review
  7. Engineering COPlant communications · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Towards engineering a hybrid carboxysome.Photosynthesis research · 2023
    Article
  12. Adapting from Low to High: An Update to COPlants (Basel, Switzerland) · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Complex structure reveals CcmM and CcmN form a heterotrimeric adaptor in β-carboxysome.Protein science : a publication of the Protein Society · 2021
    Article
  17. Review
  18. Review
  19. Article
  20. Rubisco accumulation factor 1 (Raf1) plays essential roles in mediating Rubisco assembly and carboxysome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

3 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Benedict M LongMolecular Plant Physiology Group, Research School of Biology, Australian National University, Canberra, Australian Capital Territory 0200, Australia.
Loraine Tucker
Murray R Badger
G Dean Price
Australian National University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carboxysomes are an essential part of the cyanobacterial CO2-concentrating mechanism, consisting of a protein shell and an interior of Rubisco. The beta-carboxysome shell protein CcmM forms two peptides via a proposed internal ribosomal entry site (IRES) within the ccmM transcript in Synechococcus PCC7942. The abundant short form (35 kD, M35) consists of Rubisco small subunit-like repeats and binds Rubisco. The lower abundance long form (58 kD, M58) also contains a gamma-carbonic anhydrase-like domain, which binds the carboxysomal carbonic anhydrase, CcaA. We examined whether these CcmM forms arise via an IRES or by other means. Mutations of a putative internal start codon (GTG) and Shine-Dalgarno sequence within ccmM, along with a gene coding for M35 alone, were examined in the high-CO2-requiring (HCR) carboxysomeless mutant, DeltaccmM. Expression of wild-type ccmM in DeltaccmM restored the wild-type phenotype, while mutation of putative start and Shine-Dalgarno sequences led to as much as 20-fold reduction in M35 content with no recovery from HCR phenotype. These cells also contained small electron-dense structures. Cells producing little or no M58, but sufficient M35, were found to contain large electron-dense structures, no CcaA, and had a HCR phenotype. Large subcellular aggregates can therefore form in the absence of M58, suggesting a role for M35 in internal carboxysome Rubisco packing. The results confirm that M35 is independently translated via an IRES within ccmM. Importantly, the data reveal that functional carboxysomes require both M35 and M58 in sufficient quantities and with a minimum stoichiometry of close to 1:1.

Indexed as

Bacterial ProteinsCarbon DioxideCodon, InitiatorRibulose-Bisphosphate CarboxylaseSynechococcusBacterial ProteinsCarbon DioxideCodon, InitiatorRibulose-Bisphosphate Carboxylase

Identifiers

PMID20304968
PMCPMC2862411
OpenAlexW2157692409

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.