Evidence map›Paper›PMID 32053746›Full record

ArticleMicrobiologyOpen2020

Effect of metabolosome encapsulation peptides on enzyme activity, coaggregation, incorporation, and bacterial microcompartment formation.

Rokas Juodeikis, Matthew J Lee, Matthias Mayer, Judith Mantell, Ian R Brown, Paul Verkade, Derek N Woolfson, Michael B Prentice, Stefanie Frank, Martin J Warren

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Delay-facilitated self-assembly in compartmentalized systems.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. 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

10 authors at 4 institutions in 2 countries.

Rokas JuodeikisCentre for Industrial Biotechnology, School of Biosciences, University of Kent, Canterbury, UK.
Matthew J LeeCentre for Industrial Biotechnology, School of Biosciences, University of Kent, Canterbury, UK.
Matthias MayerCentre for Industrial Biotechnology, School of Biosciences, University of Kent, Canterbury, UK.
Judith MantellSchool of Biochemistry, University of Bristol, Bristol, UK.
Ian R BrownCentre for Industrial Biotechnology, School of Biosciences, University of Kent, Canterbury, UK.
Paul VerkadeSchool of Biochemistry, University of Bristol, Bristol, UK.
Derek N WoolfsonSchool of Biochemistry, University of Bristol, Bristol, UK.
Michael B PrenticeDepartment of Microbiology, University College Cork, Cork, Ireland.
Stefanie FrankDepartment of Biochemical Engineering, University College London, London, UK.
Martin J WarrenCentre for Industrial Biotechnology, School of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-6028-6456
University of Kent · GBUniversity of Bristol · GBUniversity College Cork · IEUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/M002969/1
6 · The paper itself

Abstract

Metabolosomes, catabolic bacterial microcompartments (BMCs), are proteinaceous organelles that are associated with the breakdown of metabolites such as propanediol and ethanolamine. They are composed of an outer multicomponent protein shell that encases a specific metabolic pathway. Protein cargo found within BMCs is directed by the presence of an encapsulation peptide that appears to trigger aggregation before the formation of the outer shell. We investigated the effect of three distinct encapsulation peptides on foreign cargo in a recombinant BMC system. Our data demonstrate that these peptides cause variations in enzyme activity and protein aggregation. We observed that the level of protein aggregation generally correlates with the size of metabolosomes, while in the absence of cargo BMCs self-assemble into smaller compartments. The results agree with a flexible model for BMC formation based around the ability of the BMC shell to associate with an aggregate formed due to the interaction of encapsulation peptides.

Indexed as

BacteriaBacterial ProteinsGenes, BacterialMetabolic Networks and PathwaysMetallothioneinOrganellesPeptidesProtein TransportPyruvate DecarboxylaseRecombinant ProteinsBacterial ProteinsMetallothioneinPeptidesPyruvate DecarboxylaseRecombinant Proteinsbacterial organellescargoprotein aggregationsynthetic biologytargeting

Identifiers

PMID32053746
PMCPMC7221423
OpenAlexW3005764048

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.