Evidence map›Paper›PMID 33370261›Full record

ArticlePLoS genetics2020

MreC and MreD balance the interaction between the elongasome proteins PBP2 and RodA.

Xiaolong Liu, Jacob Biboy, Elisa Consoli, Waldemar Vollmer, Tanneke den Blaauwen

Abstract read
In one paragraph

Article in PLoS genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
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  5. The roles of theJournal of bacteriology · 2026
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  6. CoccoidVirulence · 2025
    Review
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  9. Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025
    Article
  10. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Characterization of MreCD inJournal of oral microbiology · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Comprehensive understanding of the mutant 'giant'Frontiers in plant science · 2024
    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

5 authors.

Xiaolong LiuBacterial Cell Biology & Physiology, Swammerdam Institute for Life Science, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.ORCID 0000-0002-3448-7406
Jacob BiboyCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.
Elisa ConsoliBacterial Cell Biology & Physiology, Swammerdam Institute for Life Science, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.
Waldemar VollmerCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.
Tanneke den BlaauwenBacterial Cell Biology & Physiology, Swammerdam Institute for Life Science, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.ORCID 0000-0002-5403-5597

Funding

Wellcome TrustWellcome Trust 101824/Z/13/Z
6 · The paper itself

Abstract

Rod-shape of most bacteria is maintained by the elongasome, which mediates the synthesis and insertion of peptidoglycan into the cylindrical part of the cell wall. The elongasome contains several essential proteins, such as RodA, PBP2, and the MreBCD proteins, but how its activities are regulated remains poorly understood. Using E. coli as a model system, we investigated the interactions between core elongasome proteins in vivo. Our results show that PBP2 and RodA form a complex mediated by their transmembrane and periplasmic parts and independent of their catalytic activity. MreC and MreD also interact directly with PBP2. MreC elicits a change in the interaction between PBP2 and RodA, which is suppressed by MreD. The cytoplasmic domain of PBP2 is required for this suppression. We hypothesize that the in vivo measured PBP2-RodA interaction change induced by MreC corresponds to the conformational change in PBP2 as observed in the MreC-PBP2 crystal structure, which was suggested to be the "on state" of PBP2. Our results indicate that the balance between MreC and MreD determines the activity of PBP2, which could open new strategies for antibiotic drug development.

Indexed as

Bacterial ProteinsBinding SitesEscherichia coliEscherichia coli ProteinsMembrane ProteinsPenicillin-Binding ProteinsProtein BindingBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsMrdA protein, E colimrdB protein, E coliMreC protein, BacteriaMreD protein, E coliPenicillin-Binding Proteins

Identifiers

PMID33370261
PMCPMC7793260

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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.