Evidence map›Paper›PMID 26507882›Full record

ArticleMolecular microbiology2016

Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria.

Rachel Yunck, Hongbaek Cho, Thomas G Bernhardt

Abstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing 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

80 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Comparison ofMicrobiology spectrum · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

20 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

3 authors.

Rachel YunckDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, 02115, USA.
Hongbaek ChoDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, 02115, USA.
Thomas G BernhardtDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, 02115, USA.

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Dissecting the role of YceG in E. coli cell wall biogenesisF31AI110046 · NIAID · HARVARD MEDICAL SCHOOL · PI YUNCK, RACHEL E · 2014 to 2016
$78k
NIAID NIH HHS F31 AI110046NIAID NIH HHS F31AI110046NIAID NIH HHS R01 AI083365NIAID NIH HHS R01AI083365
6 · The paper itself

Abstract

Bacterial cells are fortified against osmotic lysis by a cell wall made of peptidoglycan (PG). Synthases called penicillin-binding proteins (PBPs), the targets of penicillin and related antibiotics, polymerize the glycan strands of PG and crosslink them into the cell wall meshwork via attached peptides. The average length of glycan chains inserted into the matrix by the PBPs is thought to play an important role in bacterial morphogenesis, but polymerization termination factors controlling this process have yet to be discovered. Here, we report the identification of Escherichia coli MltG (YceG) as a potential terminase for glycan polymerization that is broadly conserved in bacteria. A clone containing mltG was initially isolated in a screen for multicopy plasmids generating a lethal phenotype in cells defective for the PG synthase PBP1b. Biochemical studies revealed that MltG is an inner membrane enzyme with endolytic transglycosylase activity capable of cleaving at internal positions within a glycan polymer. Radiolabeling experiments further demonstrated MltG-dependent nascent PG processing in vivo, and bacterial two-hybrid analysis identified an MltG-PBP1b interaction. Mutants lacking MltG were also shown to have longer glycans in their PG relative to wild-type cells. Our combined results are thus consistent with a model in which MltG associates with PG synthetic complexes to cleave nascent polymers and terminate their elongation.

Indexed as

Cell WallEndodeoxyribonucleasesEscherichia coliEscherichia coli ProteinsModels, MolecularMutationPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferasePeptidyl TransferasesPhenotypePlasmidsPolymerizationPolysaccharidesSerine-Type D-Ala-D-Ala CarboxypeptidaseEndodeoxyribonucleasesEscherichia coli Proteinspenicillin-binding protein 1B, E coliPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferasePeptidyl TransferasesPolysaccharidesSerine-Type D-Ala-D-Ala Carboxypeptidaseterminase

Identifiers

PMID26507882
PMCPMC4752859

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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.