Evidence map›Paper›PMID 31784689›Full record

ArticleScientific reports2019

Hat1 acetylates histone H4 and modulates the transcriptional program in Drosophila embryogenesis.

Júlia Varga, Szabina Korbai, Alexandra Neller, Nóra Zsindely, László Bodai

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Recent insights intoEpigenetics · 2021
    Review
  8. Review
  9. Epigenetic regulation of post-embryonic development.Current opinion in insect science · 2021
    Review
  10. Epigenetic Regulation of ALS and CMT: A Lesson fromInternational journal of molecular sciences · 2021
    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

5 authors at 1 institution in 1 country.

Júlia VargaDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, 6726, Szeged, Közép fasor 52, Hungary.
Szabina KorbaiDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, 6726, Szeged, Közép fasor 52, Hungary.
Alexandra NellerDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, 6726, Szeged, Közép fasor 52, Hungary.
Nóra ZsindelyDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, 6726, Szeged, Közép fasor 52, Hungary.
László BodaiDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, 6726, Szeged, Közép fasor 52, Hungary. bodai@bio.u-szeged.hu.ORCID http://orcid.org/0000-0001-8411-626X
University of Szeged · HU

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
NIH HHS P40 OD018537
6 · The paper itself

Abstract

Post-translational modifications of histone proteins play a pivotal role in DNA packaging and regulation of genome functions. Histone acetyltransferase 1 (Hat1) proteins are conserved enzymes that modify histones by acetylating lysine residues. Hat1 is implicated in chromatin assembly and DNA repair but its role in cell functions is not clearly elucidated. We report the generation and characterization of a Hat1 loss-of-function mutant in Drosophila. Hat1 mutants are viable and fertile with a mild sub-lethal phenotype showing that Hat1 is not essential in fruit flies. Lack of Hat1 results in the near complete loss of histone H4 lysine (K) 5 and K12 acetylation in embryos, indicating that Hat1 is the main acetyltransferase specific for these marks in this developmental stage. We found that Hat1 function and the presence of these acetyl marks are not required for the nuclear transport of histone H4 as histone variant His4r retained its nuclear localization both in Hat1 mutants and in His4r-K5R-K12R double point mutants. RNA-seq analysis of embryos indicate that in Hat1 mutants over 2000 genes are dysregulated and the observed transcriptional changes imply a delay in the developmental program of gene expression.

Indexed as

Gene Expression Regulation, DevelopmentalAcetylationAnimalsDrosophila melanogasterDrosophila ProteinsFemaleHistone AcetyltransferasesHistonesProtein Processing, Post-TranslationalTranscriptional ActivationDrosophila ProteinsHistone Acetyltransferaseshistone acetyltransferase type B complexHistones

Identifiers

PMID31784689
PMCPMC6884459
OpenAlexW2991088515

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.