Evidence map›Paper›PMID 32009249›Full record

ArticleThe EMBO journal2020

Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi-enzyme complexes in Escherichia coli.

Manuel Banzhaf, Hamish Cl Yau, Jolanda Verheul, Adam Lodge, George Kritikos, André Mateus, Baptiste Cordier, Ann Kristin Hov, Frank Stein, Morgane Wartel and 8 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.8field-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

62 citing papers in PubMed, 93 citations in OpenAlex.

  1. Peptidoglycan remodeling improves salt resilience ofApplied and environmental microbiology · 2026
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  6. JAC-antimicrobial resistance · 2025
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  14. Article
  15. Article
  16. Basal level of ppGpp coordinatesMicrobial cell (Graz, Austria) · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Review

2 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

18 authors at 5 institutions in 4 countries.

Manuel Banzhaf *European Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.
Hamish Cl Yau *Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
Jolanda Verheul *Bacterial Cell Biology & Physiology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.
Adam LodgeCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
George KritikosEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.
André MateusEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.ORCID 0000-0001-6870-0677
Baptiste CordierMicrobial Morphogenesis and Growth Lab, Institut Pasteur, Paris, France.ORCID 0000-0002-6042-9787
Ann Kristin HovEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.
Frank SteinEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.
Morgane WartelEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.
Manuel PazosCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
Alexandra S SolovyovaNewcastle University Protein and Proteome Analysis, Newcastle Upon Tyne, UK.
Eefjan BreukinkMembrane Biochemistry and Biophysics, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, The Netherlands.
Sven van TeeffelenMicrobial Morphogenesis and Growth Lab, Institut Pasteur, Paris, France.
Mikhail M SavitskiEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.ORCID 0000-0003-2011-9247
Tanneke den BlaauwenBacterial Cell Biology & Physiology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands.ORCID 0000-0002-5403-5597
Athanasios TypasEuropean Molecular Biology Laboratory, Genome Biology Unit, Heidelberg, Germany.ORCID 0000-0002-0797-9018
Waldemar VollmerCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.ORCID 0000-0003-0408-8567
European Molecular Biology Laboratory · DENewcastle University · GBInstitut Pasteur · FRUniversity of Amsterdam · NLUtrecht University · NL

Funding

Agence Nationale de la Recherche (ANR) ANR-10-LABX-62-IBEIDEC|H2020|H2020 Priority Excellent Science|H2020 European Research Council (ERC) 679980European Molecular Biology Laboratory (EMBL) 664726Medical Research Council MR/N002679/1Medical Research Council MR/N501840/1Royal Society RGS\R1\191041Volkswagen Foundation (VolkswagenStiftung)Wellcome TrustWellcome Trust (WT) 101824/Z/13/Z
6 · The paper itself

Abstract

The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identify the OM lipoprotein NlpI as a general adaptor protein for PG hydrolases. NlpI binds to different classes of hydrolases and can specifically form complexes with various PG endopeptidases. In addition, NlpI seems to contribute both to PG elongation and division biosynthetic complexes based on its localization and genetic interactions. Consistent with such a role, we reconstitute PG multi-enzyme complexes containing NlpI, the PG synthesis regulator LpoA, its cognate bifunctional synthase, PBP1A, and different endopeptidases. Our results indicate that peptidoglycan regulators and adaptors are part of PG biosynthetic multi-enzyme complexes, regulating and potentially coordinating the spatiotemporal action of PG synthases and hydrolases.

Indexed as

Multienzyme ComplexesCell WallEndopeptidasesEscherichia coliEscherichia coli ProteinsLipoproteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanEndopeptidasesEscherichia coli ProteinsLipoproteinsMultienzyme ComplexesN-Acetylmuramoyl-L-alanine AmidaseNlpI protein, E coliPeptidoglycanpeptidoglycan endopeptidasebacterial cell envelopeendopeptidaseouter membrane lipoproteinpenicillin-binding proteinpeptidoglycan

Identifiers

PMID32009249
PMCPMC7049810
OpenAlexW3003362316

What OpenQuestion holds

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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.