Evidence map›Paper›PMID 26804901›Full record

ArticleCell reports2016

Operon Gene Order Is Optimized for Ordered Protein Complex Assembly.

Jonathan N Wells, L Therese Bergendahl, Joseph A Marsh

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Discovering optimal kinetic pathways for self-assembly using automatic differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. c-di-AMP determines the hierarchical organization of bacterial RCK proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. New algorithms for structure informed genome rearrangement.Algorithms for molecular biology : AMB · 2023
    Article
  9. Article
  10. Article
  11. Architecture and genomic arrangement of the MurE-MurF bacterial cell wall biosynthesis complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Review
  13. Article
  14. Article
  15. Solid-Phase Cell-Free Protein Synthesis and Its Applications in Biotechnology.Advances in biochemical engineering/biotechnology · 2023
    Article
  16. Article
  17. Article
  18. Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

3 authors at 3 institutions in 1 country.

Jonathan N WellsMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, United Kingdom.
L Therese BergendahlMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, United Kingdom.
Joseph A MarshMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, United Kingdom. Electronic address: joseph.marsh@igmm.ed.ac.uk.
MRC Institute of Genetics and Molecular Medicine · GBUniversity of Edinburgh · GBWestern General Hospital · GB

Funding

Medical Research Council MR/M02122X/1
6 · The paper itself

Abstract

The assembly of heteromeric protein complexes is an inherently stochastic process in which multiple genes are expressed separately into proteins, which must then somehow find each other within the cell. Here, we considered one of the ways by which prokaryotic organisms have attempted to maximize the efficiency of protein complex assembly: the organization of subunit-encoding genes into operons. Using structure-based assembly predictions, we show that operon gene order has been optimized to match the order in which protein subunits assemble. Exceptions to this are almost entirely highly expressed proteins for which assembly is less stochastic and for which precisely ordered translation offers less benefit. Overall, these results show that ordered protein complex assembly pathways are of significant biological importance and represent a major evolutionary constraint on operon gene organization.

Indexed as

Gene OrderGenes, BacterialOperonProtein MultimerizationAmino Acid SequenceBacterial ProteinsMolecular Sequence DataProtein BindingBacterial Proteins

Identifiers

PMID26804901
PMCPMC4742563
OpenAlexW2265278721

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.