Evidence map›Paper›PMID 26148529›Full record

ReviewMolecular microbiology2015

Bacterial microcompartments: widespread prokaryotic organelles for isolation and optimization of metabolic pathways.

Thomas A Bobik, Brent P Lehman, Todd O Yeates

Abstract readReview
In one paragraph

Review in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Isolation and Visualization Fusobacterium nucleatum Microcompartments.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024
    Review
  7. Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024
    Review
  8. Article
  9. Ethanolamine-induced assembly of microcompartments is required forbioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Review
  14. Article
  15. Encapsulins.Annual review of biochemistry · 2022
    Review
  16. Article
  17. A synthetic bacterial microcompartment as production platform for pyruvate from formate and acetate.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  20. Article

15 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

3 authors.

Thomas A BobikRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, 50011, USA.
Brent P LehmanRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, 50011, USA.
Todd O YeatesMolecular Biology Institute, University of California, Los Angeles, CA, USA.

Funding

Dissecting the structure, function, and mechanisms of diverse protein-based metabolic organelles in bacteriaR01AI081146 · NIAID · IOWA STATE UNIVERSITY · PI BOBIK, THOMAS AQUINAS, YEATES, TODD O · 2009 to 2022
$6.5M
NIAID NIH HHS R01 AI081146NIAID NIH HHS R01AI081146
6 · The paper itself

Abstract

Prokaryotes use subcellular compartments for a variety of purposes. An intriguing example is a family of complex subcellular organelles known as bacterial microcompartments (MCPs). MCPs are widely distributed among bacteria and impact processes ranging from global carbon fixation to enteric pathogenesis. Overall, MCPs consist of metabolic enzymes encased within a protein shell, and their function is to optimize biochemical pathways by confining toxic or volatile metabolic intermediates. MCPs are fundamentally different from other organelles in having a complex protein shell rather than a lipid-based membrane as an outer barrier. This unusual feature raises basic questions about organelle assembly, protein targeting and metabolite transport. In this review, we discuss the three best-studied MCPs highlighting atomic-level models for shell assembly, targeting sequences that direct enzyme encapsulation, multivalent proteins that organize the lumen enzymes, the principles of metabolite movement across the shell, internal cofactor recycling, a potential system of allosteric regulation of metabolite transport and the mechanism and rationale behind the functional diversification of the proteins that form the shell. We also touch on some potential biotechnology applications of an unusual compartment designed by nature to optimize metabolic processes within a cellular context.

Indexed as

Metabolic Networks and PathwaysBacteriaBacterial ProteinsCell CompartmentationBacterial Proteins

Identifiers

PMID26148529
PMCPMC4718714

What OpenQuestion holds

Textmetadata
LicenceTDM
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.