Evidence map›Paper›PMID 32710625›Full record

ArticleNucleic acids research2020

Alternative linker histone permits fast paced nuclear divisions in early Drosophila embryo.

László Henn, Anikó Szabó, László Imre, Ádám Román, Andrea Ábrahám, Balázs Vedelek, Péter Nánási, Imre M Boros

Abstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Nucleosome destabilization by polyamines.Archives of biochemistry and biophysics · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. 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

8 authors.

László HennInstitute of Biochemistry, Biological Research Centre of Szeged, Szeged H-6726, Hungary.
Anikó SzabóInstitute of Biochemistry, Biological Research Centre of Szeged, Szeged H-6726, Hungary.
László ImreDepartment of Biophysics and Cell Biology, University of Debrecen, Debrecen H-4032 Hungary.
Ádám RománDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Szeged H-6726, Hungary.
Andrea ÁbrahámInstitute of Biochemistry, Biological Research Centre of Szeged, Szeged H-6726, Hungary.
Balázs VedelekDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Szeged H-6726, Hungary.
Péter NánásiDepartment of Biophysics and Cell Biology, University of Debrecen, Debrecen H-4032 Hungary.
Imre M BorosInstitute of Biochemistry, Biological Research Centre of Szeged, Szeged H-6726, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In most animals, the start of embryogenesis requires specific histones. In Drosophila linker histone variant BigH1 is present in early embryos. To uncover the specific role of this alternative linker histone at early embryogenesis, we established fly lines in which domains of BigH1 have been replaced partially or completely with that of H1. Analysis of the resulting Drosophila lines revealed that at normal temperature somatic H1 can substitute the alternative linker histone, but at low temperature the globular and C-terminal domains of BigH1 are essential for embryogenesis. In the presence of BigH1 nucleosome stability increases and core histone incorporation into nucleosomes is more rapid, while nucleosome spacing is unchanged. Chromatin formation in the presence of BigH1 permits the fast-paced nuclear divisions of the early embryo. We propose a model which explains how this specific linker histone ensures the rapid nucleosome reassembly required during quick replication cycles at the start of embryogenesis.

Indexed as

Cell Nucleus DivisionAnimalsChromatinChromatin Assembly and DisassemblyDrosophilaDrosophila ProteinsEmbryonic DevelopmentEmbryo, NonmammalianHistonesNucleosomesBigH1 protein, DrosophilaChromatinDrosophila ProteinsHistonesNucleosomes

Identifiers

PMID32710625
PMCPMC7498357

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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.