Evidence map›Paper›PMID 27063436›Full record

ArticleScientific reports2016

Engineering formation of multiple recombinant Eut protein nanocompartments in E. coli.

Mark Held, Alexander Kolb, Sarah Perdue, Szu-Yi Hsu, Sarah E Bloch, Maureen B Quin, Claudia Schmidt-Dannert

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Ethanolamine-induced assembly of microcompartments is required forbioRxiv : the preprint server for biology · 2024
    Article
  6. IntegrativemSystems · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021
    Review
  12. Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. 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

7 authors.

Mark HeldDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.
Alexander KolbDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.
Sarah PerdueDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.
Szu-Yi HsuDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.
Sarah E BlochDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.
Maureen B QuinDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.
Claudia Schmidt-DannertDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Compartmentalization of designed metabolic pathways within protein based nanocompartments has the potential to increase reaction efficiency in multi-step biosynthetic reactions. We previously demonstrated proof-of-concept of this aim by targeting a functional enzyme to single cellular protein nanocompartments, which were formed upon recombinant expression of the Salmonella enterica LT2 ethanolamine utilization bacterial microcompartment shell proteins EutS or EutSMNLK in Escherichia coli. To optimize this system, increasing overall encapsulated enzyme reaction efficiency, factor(s) required for the production of more than one nanocompartment per cell must be identified. In this work we report that the cupin domain protein EutQ is required for assembly of more than one nanocompartment per cell. Overexpression of EutQ results in multiple nanocompartment assembly in our recombinant system. EutQ specifically interacts with the shell protein EutM in vitro via electrostatic interactions with the putative cytosolic face of EutM. These findings lead to the theory that EutQ could facilitate multiple nanocompartment biogenesis by serving as an assembly hub for shell proteins. This work offers insights into the biogenesis of Eut bacterial microcompartments, and also provides an improved platform for the production of protein based nanocompartments for targeted encapsulation of enzyme pathways.

Indexed as

Bacterial ProteinsEscherichia coliEthanolamineGenetic EngineeringMetabolic Networks and PathwaysMicroscopy, Electron, TransmissionMicroscopy, FluorescencePlasmidsProtein Structure, TertiaryRecombinant ProteinsSalmonella entericaTime-Lapse ImagingBacterial ProteinsEthanolamineRecombinant Proteins

Identifiers

PMID27063436
PMCPMC4827028

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Registered trials

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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.