Evidence map›Paper›PMID 33006967›Full record

ArticlePloS one2020

Morphological peculiarities of the DNA-protein complexes in starved Escherichia coli cells.

Natalia Loiko, Yana Danilova, Andrey Moiseenko, Vladislav Kovalenko, Ksenia Tereshkina, Maria Tutukina, Galina El-Registan, Olga Sokolova, Yurii Krupyanskii

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.4field-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

16 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural and Binding Properties of Dps - A Nucleoid Associated Protein.bioRxiv : the preprint server for biology · 2025
    Article
  4. The Dps Protein ProtectsInternational journal of molecular sciences · 2025
    Article
  5. Article
  6. Article
  7. Bridging DNA contacts allow Dps frombioRxiv : the preprint server for biology · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Pathological ATX3 Expression Induces Cell Perturbations inInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. 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

9 authors at 4 institutions in 2 countries.

Natalia LoikoDepartment of Structure of Matter, Semenov Federal Research Center of Chemical Physics, RAS, Moscow, Russia.
Yana DanilovaDepartment of Biology, Lomonosov Moscow State University, Faculty of Biology, Moscow, Russia.
Andrey MoiseenkoDepartment of Structure of Matter, Semenov Federal Research Center of Chemical Physics, RAS, Moscow, Russia.
Vladislav KovalenkoDepartment of Structure of Matter, Semenov Federal Research Center of Chemical Physics, RAS, Moscow, Russia.
Ksenia TereshkinaDepartment of Structure of Matter, Semenov Federal Research Center of Chemical Physics, RAS, Moscow, Russia.
Maria TutukinaCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.
Galina El-RegistanDepartment of Microbiology, Federal Research Center 'Fundamentals of Biotechnology' RAS, Moscow, Russia.
Olga SokolovaDepartment of Biology, Lomonosov Moscow State University, Faculty of Biology, Moscow, Russia.
Yurii KrupyanskiiDepartment of Structure of Matter, Semenov Federal Research Center of Chemical Physics, RAS, Moscow, Russia.ORCID 0000-0002-2994-4799
Semenov Institute of Chemical Physics · RULomonosov Moscow State University · RUFederal Research Centre «Fundamentals of Biotechnology» of the Russian Academy of Sciences · RUSkolkovo Institute of Science and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the adaptive strategies for the constantly changing conditions of the environment utilized in bacterial cells involves the condensation of DNA in complex with the DNA-binding protein, Dps. With the use of electron microscopy and electron tomography, we observed several morphologically different types of DNA condensation in dormant Escherichia coli cells, namely: nanocrystalline, liquid crystalline, and the folded nucleosome-like. We confirmed the presence of both Dps and DNA in all of the ordered structures using EDX analysis. The comparison of EDX spectra obtained for the three different ordered structures revealed that in nanocrystalline formation the majority of the Dps protein is tightly bound to nucleoid DNA. The dps-null cells contained only one type of condensed DNA structure, liquid crystalline, thus, differing from those with Dps. The results obtained here shed some light on the phenomenon of DNA condensation in dormant prokaryotic cells and on the general problem of developing a response to stress. We demonstrated that the population of dormant cells is structurally heterogeneous, allowing them to respond flexibly to environmental changes. It increases the ability of the whole bacterial population to survive under extreme stress conditions.

Indexed as

DNA, BacterialDNA-Binding ProteinsDNA PackagingEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialMicroscopy, ElectronModels, MolecularNucleic Acid ConformationStress, PhysiologicalDNA, BacterialDNA-Binding ProteinsEscherichia coli Proteins

Identifiers

PMID33006967
PMCPMC7531825
OpenAlexW3090631012

What OpenQuestion holds

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LicenceCC BY
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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.