Evidence map›Paper›PMID 30061355›Full record

ArticleJournal of bacteriology2018

High-Resolution Analysis of the Peptidoglycan Composition in Streptomyces coelicolor.

Lizah T van der Aart, Gerwin K Spijksma, Amy Harms, Waldemar Vollmer, Thomas Hankemeier, Gilles P van Wezel

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

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  15. Alterations in the Cell Wall ofFrontiers in microbiology · 2020
    Article
  16. Ultrastructure of Exospore Formation inFrontiers in microbiology · 2020
    Article
  17. Article
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  19. Review
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

6 authors at 2 institutions in 2 countries.

Lizah T van der AartMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.
Gerwin K SpijksmaDivision of Analytical Biosciences, Leiden Academic Center for Drug Research, Leiden University, Leiden, The Netherlands.
Amy HarmsDivision of Analytical Biosciences, Leiden Academic Center for Drug Research, Leiden University, Leiden, The Netherlands.
Waldemar VollmerCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Thomas HankemeierDivision of Analytical Biosciences, Leiden Academic Center for Drug Research, Leiden University, Leiden, The Netherlands.
Gilles P van WezelMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands g.wezel@biology.leidenuniv.nl.ORCID 0000-0003-0341-1561
Leiden University · NLNewcastle University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial cell wall maintains cell shape and protects against bursting by turgor. A major constituent of the cell wall is peptidoglycan (PG), which is continuously modified to enable cell growth and differentiation through the concerted activity of biosynthetic and hydrolytic enzymes. Streptomycetes are Gram-positive bacteria with a complex multicellular life style alternating between mycelial growth and the formation of reproductive spores. This involves cell wall remodeling at apical sites of the hyphae during cell elongation and autolytic degradation of the vegetative mycelium during the onset of development and antibiotic production. Here, we show that there are distinct differences in the cross-linking and maturation of the PGs between exponentially growing vegetative hyphae and the aerial hyphae that undergo sporulation. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis identified over 80 different muropeptides, revealing that major PG hydrolysis takes place over the course of mycelial growth. Half of the dimers lacked one of the disaccharide units in transition-phase cells, most likely due to autolytic activity. The deacetylation of MurNAc to MurN was particularly pronounced in spores and strongly reduced in sporulation mutants with a deletion of

Indexed as

Bacterial ProteinsCell WallChromatography, LiquidHydrolysisHyphaePeptidoglycanSpores, BacterialStreptomyces coelicolorTandem Mass SpectrometryBacterial ProteinsPeptidoglycancell wallmass spectrometrymulticellular growthprogrammed cell deathsporulationStreptomyces

Identifiers

PMID30061355
PMCPMC6153666
OpenAlexW2800141991

What OpenQuestion holds

Textmetadata
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.