Evidence map›Paper›PMID 33278861›Full record

ArticleMolecular microbiology2021

MltG activity antagonizes cell wall synthesis by both types of peptidoglycan polymerases in Escherichia coli.

Jessica L Bohrhunter, Patricia D A Rohs, Grasiela Torres, Rachel Yunck, Thomas G Bernhardt

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Mutation ofJournal of bacteriology · 2023
    Article
  10. Mutation ofbioRxiv : the preprint server for biology · 2023
    Article
  11. Enhanced Cell Wall and Cell Membrane Activity Promotes Heat Adaptation ofInternational journal of molecular sciences · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Biochemical reconstitution defines new functions for membrane-bound glycosidases in assembly of the bacterial cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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 at 2 institutions in 1 country.

Jessica L BohrhunterDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Patricia D A RohsDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Grasiela TorresDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Rachel YunckDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.
Thomas G BernhardtDepartment of Microbiology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0003-3566-7756
Harvard University · USHoward Hughes Medical Institute · US

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Dissecting the role of Escherichia coli peptidoglycan synthase activatorsF31AI122363 · NIAID · HARVARD MEDICAL SCHOOL · PI BOHRHUNTER, JESSICA L · 2016 to 2018
$99k
Howard Hughes Medical InstituteNIAID NIH HHS F31 AI122363NIAID NIH HHS R01 AI083365
6 · The paper itself

Abstract

Bacterial cells are surrounded by a peptidoglycan (PG) cell wall. This structure is essential for cell integrity and its biogenesis pathway is a key antibiotic target. Most bacteria utilize two types of synthases that polymerize glycan strands and crosslink them: class A penicillin-binding proteins (aPBPs) and complexes of SEDS proteins and class B PBPs (bPBPs). Although the enzymatic steps of PG synthesis are well characterized, the steps involved in terminating PG glycan polymerization remain poorly understood. A few years ago, the conserved lytic transglycosylase MltG was identified as a potential terminase for PG synthesis in Escherichia coli. However, characterization of the in vivo function of MltG was hampered by the lack of a growth or morphological phenotype in ΔmltG cells. Here, we report the isolation of MltG-defective mutants as suppressors of lethal deficits in either aPBP or SEDS/bPBP PG synthase activity. We used this phenotype to perform a domain-function analysis for MltG, which revealed that access to the inner membrane is important for its in vivo activity. Overall, our results support a model in which MltG functions as a terminase for both classes of PG synthases by cleaving PG glycans as they are being actively synthesized.

Indexed as

Cell WallEndodeoxyribonucleasesEscherichia coliEscherichia coli ProteinsPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferaseEndodeoxyribonucleasesEscherichia coli ProteinsPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan Glycosyltransferaseterminasecell envelopecell walllytic transglycosylasepenicillinpeptidoglycan

Identifiers

PMID33278861
PMCPMC9020800
OpenAlexW3111178647

What OpenQuestion holds

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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.