Evidence map›Paper›PMID 33666292›Full record

ArticleMolecular microbiology2021

The active repertoire of Escherichia coli peptidoglycan amidases varies with physiochemical environment.

Elizabeth A Mueller, Abbygail G Iken, Mehmet Ali Öztürk, Matthias Winkle, Mirko Schmitz, Waldemar Vollmer, Barbara Di Ventura, Petra Anne Levin

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
5.7field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Modelling host-pathogen interactions:Microbiology (Reading, England) · 2025
    Article
  6. Review
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  8. Article
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  12. Activator-induced conformational changes regulate division-associated peptidoglycan amidases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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

8 authors at 3 institutions in 3 countries.

Elizabeth A MuellerDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Abbygail G IkenDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Mehmet Ali ÖztürkSignalling Research Centers BIOSS and CIBSS, McKelvey School of Engineering, University of Freiburg, Freiburg, Germany.
Matthias WinkleThe Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, UK.
Mirko SchmitzSignalling Research Centers BIOSS and CIBSS, McKelvey School of Engineering, University of Freiburg, Freiburg, Germany.
Waldemar VollmerThe Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, UK.
Barbara Di VenturaSignalling Research Centers BIOSS and CIBSS, McKelvey School of Engineering, University of Freiburg, Freiburg, Germany.
Petra Anne LevinDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID 0000-0003-2071-0547
University of Freiburg · DEWashington University in St. Louis · USCentre for Life · GB

Funding

HOMEOSTATIC CONTROL OF BACTERIAL GROWTH AND CELL DIVISIONR35GM127331 · NIGMS · WASHINGTON UNIVERSITY · PI Petra Anne Levin · 2018 to 2026
$4.3M
NIGMS NIH HHS R35 GM127331
6 · The paper itself

Abstract

Nearly all bacteria are encased in peptidoglycan, an extracytoplasmic matrix of polysaccharide strands crosslinked through short peptide stems. In the Gram-negative model organism Escherichia coli, more than 40 synthases and autolysins coordinate the growth and division of the peptidoglycan sacculus in the periplasm. The precise contribution of many of these enzymes to peptidoglycan metabolism remains unclear due to significant apparent redundancy, particularly among the autolysins. E. coli produces three major LytC-type-N-acetylmuramoyl-L-alanine amidases, which share a role in separating the newly formed daughter cells during cytokinesis. Here, we reveal two of the three amidases that exhibit growth medium-dependent changes in activity. Specifically, we report acidic growth conditions stimulate AmiB-and to a lesser extent, AmiC-amidase activity. Combining genetic, biochemical, and computational analyses, we demonstrate that low pH-dependent stimulation of AmiB is mediated through the periplasmic amidase activators NlpD, EnvC, and ActS (formerly known as YgeR). Although NlpD and EnvC promote amidase activity across pH environments, ActS preferentially stimulates AmiB activity in acidic conditions. Altogether, our findings support partially overlapping roles for E. coli amidases and their regulators in cell separation and illuminate the physiochemical environment as an important mediator of cell wall enzyme activity.

Indexed as

Bacterial ProteinsCell WallEndopeptidasesEscherichia coliEscherichia coli ProteinsLipoproteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanBacterial ProteinsEndopeptidasesEnvC protein, E coliEscherichia coli ProteinsLipoproteinsN-Acetylmuramoyl-L-alanine AmidaseNlpD protein, bacteriaPeptidoglycanamidasescytokinesismorphogenesispeptidoglycanpH

Identifiers

PMID33666292
PMCPMC8295211
OpenAlexW3135342450

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.