Evidence map›Paper›PMID 37877652›Full record

ArticleMicrobiologyOpen2023

Relationship between the Rod complex and peptidoglycan structure in Escherichia coli.

Risa Ago, Yuhei O Tahara, Honoka Yamaguchi, Motoya Saito, Wakana Ito, Kaito Yamasaki, Taishi Kasai, Sho Okamoto, Taiki Chikada, Taku Oshima and 4 more

Abstract read
In one paragraph

Article in MicrobiologyOpen, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanics ofMolecular biology of the cell · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Comprehensive understanding of the mutant 'giant'Frontiers in plant science · 2024
    Article
  13. 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

14 authors.

Risa AgoDepartment of Life Science, College of Science, Rikkyo University, Tokyo, Japan.
Yuhei O TaharaGraduate School of Science, Osaka Metropolitan University, Osaka, Japan.ORCID 0000-0002-2736-9233
Honoka YamaguchiDepartment of Life Science, College of Science, Rikkyo University, Tokyo, Japan.
Motoya SaitoDepartment of Biotechnology, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan.
Wakana ItoDepartment of Biotechnology, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan.
Kaito YamasakiDepartment of Pharmaceutical Engineering, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan.
Taishi KasaiDepartment of Life Science, College of Science, Rikkyo University, Tokyo, Japan.ORCID 0000-0002-6600-5184
Sho OkamotoMicrobial Physiology Laboratory, Department of Gene Function and Phenomics, National Institute of Genetics, Mishima, Shizuoka, Japan.
Taiki ChikadaDepartment of Life Science, College of Science, Rikkyo University, Tokyo, Japan.
Taku OshimaDepartment of Biotechnology, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0002-0949-5543
Issey OsakaDepartment of Pharmaceutical Engineering, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan.ORCID 0000-0002-3642-2278
Makoto MiyataGraduate School of Science, Osaka Metropolitan University, Osaka, Japan.ORCID 0000-0002-7478-7390
Hironori NikiMicrobial Physiology Laboratory, Department of Gene Function and Phenomics, National Institute of Genetics, Mishima, Shizuoka, Japan.ORCID 0000-0002-5391-6595
Daisuke ShiomiDepartment of Life Science, College of Science, Rikkyo University, Tokyo, Japan.ORCID 0000-0002-8558-7175

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidoglycan for elongation in Escherichia coli is synthesized by the Rod complex, which includes RodZ. Although various mutant strains of the Rod complex have been isolated, the relationship between the activity of the Rod complex and the overall physical and chemical structures of the peptidoglycan have not been reported. We constructed a RodZ mutant, termed RMR, and analyzed the growth rate, morphology, and other characteristics of cells producing the Rod complexes containing RMR. The growth and morphology of RMR cells were abnormal, and we isolated suppressor mutants from RMR cells. Most of the suppressor mutations were found in components of the Rod complex, suggesting that these suppressor mutations increase the integrity and/or the activity of the Rod complex. We purified peptidoglycan from wild-type, RMR, and suppressor mutant cells and observed their structures in detail. We found that the peptidoglycan purified from RMR cells had many large holes and different compositions of muropeptides from those of WT cells. The Rod complex may be a determinant not only for the whole shape of peptidoglycan but also for its highly dense structure to support the mechanical strength of the cell wall.

Indexed as

Escherichia coliEscherichia coli ProteinsCell WallCytoskeletal ProteinsPeptidoglycanCytoskeletal ProteinsEscherichia coli ProteinsPeptidoglycanRodZ protein, E colicell shapepeptidoglycanRod complexsuppressor mutation

Identifiers

PMID37877652
PMCPMC10561026

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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.