Evidence map›Paper›PMID 26867711›Full record

ArticleScientific reports2016

Characterization of SCO4439, a D-alanyl-D-alanine carboxypeptidase involved in spore cell wall maturation, resistance, and germination in Streptomyces coelicolor.

Beatriz Rioseras, Paula Yagüe, María Teresa López-García, Nathaly Gonzalez-Quiñonez, Elisa Binda, Flavia Marinelli, Angel Manteca

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.9field-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

22 citing papers in PubMed, 31 citations in OpenAlex.

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  18. Quantitative Proteome and Phosphoproteome Analyses ofMolecular & cellular proteomics : MCP · 2018
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  19. Review
  20. Frontiers in cellular and infection microbiology · 2018
    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

7 authors at 2 institutions in 2 countries.

Beatriz RioserasÁrea de Microbiología, Departamento de Biología Funcional and IUOPA, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain.
Paula YagüeÁrea de Microbiología, Departamento de Biología Funcional and IUOPA, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain.
María Teresa López-GarcíaÁrea de Microbiología, Departamento de Biología Funcional and IUOPA, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain.
Nathaly Gonzalez-QuiñonezÁrea de Microbiología, Departamento de Biología Funcional and IUOPA, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain.
Elisa BindaDepartment of Biotechnology and Life Sciences, University of Insubria, via J. H. Dunant 3, 21100 Varese, Italy.
Flavia MarinelliDepartment of Biotechnology and Life Sciences, University of Insubria, via J. H. Dunant 3, 21100 Varese, Italy.
Angel MantecaÁrea de Microbiología, Departamento de Biología Funcional and IUOPA, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain.
Universidad de Oviedo · ESUniversity of Insubria · IT

Funding

European Research Council 280304
6 · The paper itself

Abstract

This work contributes to the understanding of cell wall modifications during sporulation and germination in Streptomyces by assessing the biological function and biochemical properties of SCO4439, a D-alanyl-D-alanine carboxypeptidase (DD-CPase) constitutively expressed during development. SCO4439 harbors a DD-CPase domain and a putative transcriptional regulator domain, separated by a putative transmembrane region. The recombinant protein shows that DD-CPase activity is inhibited by penicillin G. The spores of the SCO4439::Tn5062 mutant are affected in their resistance to heat and acid and showed a dramatic increase in swelling during germination. The mycelium of the SCO4439::Tn5062 mutant is more sensitive to glycopeptide antibiotics (vancomycin and teicoplanin). The DD-CPase domain and the hydrophobic transmembrane region are highly conserved in Streptomyces, and both are essential for complementing the wild type phenotypes in the mutant. A model for the biological mechanism behind the observed phenotypes is proposed, in which SCO4439 DD-CPase releases D-Ala from peptidoglycan (PG) precursors, thereby reducing the substrate pool for PG crosslinking (transpeptidation). PG crosslinking regulates spore physical resistance and germination, and modulates mycelium resistance to glycopeptides. This study is the first demonstration of the role of a DD-CPase in the maturation of the spore cell wall.

Indexed as

Cell WallConserved SequenceGene Knockout TechniquesPenicillin GProtease InhibitorsProtein DomainsSerine-Type D-Ala-D-Ala CarboxypeptidaseSpores, BacterialStreptomyces coelicolorPenicillin GProtease InhibitorsSerine-Type D-Ala-D-Ala Carboxypeptidase

Identifiers

PMID26867711
PMCPMC4751497
OpenAlexW2294146745

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.