Evidence map›Paper›PMID 32332738›Full record

ArticleNature communications2020

Decoding the stoichiometric composition and organisation of bacterial metabolosomes.

Mengru Yang, Deborah M Simpson, Nicolas Wenner, Philip Brownridge, Victoria M Harman, Jay C D Hinton, Robert J Beynon, Lu-Ning Liu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024
    Review
  18. Article
  19. IntegrativemSystems · 2024
    Article
  20. Electrochemical cofactor recycling of bacterial microcompartments.bioRxiv : the preprint server for biology · 2024
    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

8 authors at 1 institution in 2 countries.

Mengru YangInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Deborah M SimpsonInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.ORCID http://orcid.org/0000-0002-3962-4895
Nicolas WennerInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Philip BrownridgeInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Victoria M HarmanInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Jay C D HintonInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Robert J BeynonInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Lu-Ning LiuInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK. luning.liu@liverpool.ac.uk.ORCID http://orcid.org/0000-0002-8884-4819
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M024202/1Biotechnology and Biological Sciences Research Council BB/R003890/1Wellcome TrustWellcome Trust 106914/Z/15/Z
6 · The paper itself

Abstract

Some enteric bacteria including Salmonella have evolved the propanediol-utilising microcompartment (Pdu MCP), a specialised proteinaceous organelle that is essential for 1,2-propanediol degradation and enteric pathogenesis. Pdu MCPs are a family of bacterial microcompartments that are self-assembled from hundreds of proteins within the bacterial cytosol. Here, we seek a comprehensive understanding of the stoichiometric composition and organisation of Pdu MCPs. We obtain accurate stoichiometry of shell proteins and internal enzymes of the natural Pdu MCP by QconCAT-driven quantitative mass spectrometry. Genetic deletion of the major shell protein and absolute quantification reveal the stoichiometric and structural remodelling of metabolically functional Pdu MCPs. Decoding the precise protein stoichiometry allows us to develop an organisational model of the Pdu metabolosome. The structural insights into the Pdu MCP are critical for both delineating the general principles underlying bacterial organelle formation, structural robustness and function, and repurposing natural microcompartments using synthetic biology for biotechnological applications.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsBiotechnologyCatalysisCytoplasmGreen Fluorescent ProteinsMass SpectrometryMetabolomicsMutationPropylene GlycolProtein ConformationProteomicsSalmonella entericaSalmonella typhimuriumSynthetic BiologyBacterial ProteinsGreen Fluorescent ProteinsPropylene Glycol

Identifiers

PMID32332738
PMCPMC7181861
OpenAlexW3020192812

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.