Evidence map›Paper›PMID 26243377›Full record

ArticleScientific reports2015

Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module.

Joel Selkrig, Matthew J Belousoff, Stephen J Headey, Eva Heinz, Takuya Shiota, Hsin-Hui Shen, Simone A Beckham, Rebecca S Bamert, Minh-Duy Phan, Mark A Schembri and 4 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. YdbL directly modulates YdbH-YnbE bridge formation to maintainbioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Polydextrose reduces the infection ofMicrobiology spectrum · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

14 authors at 3 institutions in 1 country.

Joel Selkrig1] Department of Microbiology, Monash University, Clayton 3800, Australia [2] Department of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia.
Matthew J BelousoffDepartment of Microbiology, Monash University, Clayton 3800, Australia.
Stephen J HeadeyMedicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville 3052, Australia.
Eva HeinzDepartment of Microbiology, Monash University, Clayton 3800, Australia.
Takuya ShiotaDepartment of Microbiology, Monash University, Clayton 3800, Australia.
Hsin-Hui Shen1] Department of Microbiology, Monash University, Clayton 3800, Australia [2] Department of Materials Engineering, Monash University, Clayton 3800, Australia.
Simone A BeckhamDepartment of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia.
Rebecca S BamertDepartment of Microbiology, Monash University, Clayton 3800, Australia.
Minh-Duy PhanAustralian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia.
Mark A SchembriAustralian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia.
Matthew C J WilceDepartment of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia.
Martin J ScanlonMedicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville 3052, Australia.
Richard A StrugnellDepartment of Microbiology &Immunology, University of Melbourne, Parkville 3052, Australia.
Trevor LithgowDepartment of Microbiology, Monash University, Clayton 3800, Australia.
Monash University · AUUniversity of Queensland · AUUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biogenesis of membranes from constituent proteins and lipids is a fundamental aspect of cell biology. In the case of proteins assembled into bacterial outer membranes, an overarching question concerns how the energy required for protein insertion and folding is accessed at this remote location of the cell. The translocation and assembly module (TAM) is a nanomachine that functions in outer membrane biogenesis and virulence in diverse bacterial pathogens. Here we demonstrate the interactions through which TamA and TamB subunits dock to bridge the periplasm, and unite the outer membrane aspects to the inner membrane of the bacterial cell. We show that specific functional features in TamA have been conserved through evolution, including residues surrounding the lateral gate and an extensive surface of the POTRA domains. Analysis by nuclear magnetic resonance spectroscopy and small angle X-ray scattering document the characteristic structural features of these POTRA domains and demonstrate rigidity in solution. Quartz crystal microbalance measurements pinpoint which POTRA domain specifically docks the TamB subunit of the nanomachine. We speculate that the POTRA domain of TamA functions as a lever arm in order to drive the activity of the TAM, assembling proteins into bacterial outer membranes.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsConserved SequenceEvolution, MolecularModels, MolecularMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein Structure, SecondaryBacterial Outer Membrane Proteins

Identifiers

PMID26243377
PMCPMC4525385
OpenAlexW1075008563

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.