Evidence map›Paper›PMID 32198348›Full record

ArticleNature communications2020

Distinct roles for H4 and H2A.Z acetylation in RNA transcription in African trypanosomes.

Amelie J Kraus, Jens T Vanselow, Stephanie Lamer, Benedikt G Brink, Andreas Schlosser, T Nicolai Siegel

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.7field-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

28 citing papers in PubMed, 59 citations in OpenAlex.

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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 1 country.

Amelie J KrausDepartment of Veterinary Sciences, Experimental Parasitology, Ludwig-Maximilians-Universität München, 80752, Munich, Germany.ORCID http://orcid.org/0000-0002-4406-0721
Jens T VanselowRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080, Würzburg, Germany.
Stephanie LamerRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080, Würzburg, Germany.
Benedikt G BrinkDepartment of Veterinary Sciences, Experimental Parasitology, Ludwig-Maximilians-Universität München, 80752, Munich, Germany.ORCID http://orcid.org/0000-0002-2291-8870
Andreas SchlosserRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080, Würzburg, Germany.
T Nicolai SiegelDepartment of Veterinary Sciences, Experimental Parasitology, Ludwig-Maximilians-Universität München, 80752, Munich, Germany. n.siegel@lmu.de.ORCID http://orcid.org/0000-0002-1715-7907
University of Würzburg · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite histone H2A variants and acetylation of histones occurring in almost every eukaryotic organism, it has been difficult to establish direct functional links between canonical histones or H2A variant acetylation, deposition of H2A variants and transcription. To disentangle these complex interdependent processes, we devised a highly sensitive strategy for quantifying histone acetylation levels at specific genomic loci. Taking advantage of the unusual genome organization in Trypanosoma brucei, we identified 58 histone modifications enriched at transcription start sites (TSSs). Furthermore, we found TSS-associated H4 and H2A.Z acetylation to be mediated by two different histone acetyltransferases, HAT2 and HAT1, respectively. Whereas depletion of HAT2 decreases H2A.Z deposition and shifts the site of transcription initiation, depletion of HAT1 does not affect H2A.Z deposition but reduces total mRNA levels by 50%. Thus, specifically reducing H4 or H2A.Z acetylation levels enabled us to reveal distinct roles for these modifications in H2A.Z deposition and RNA transcription.

Indexed as

Protein Processing, Post-TranslationalAcetylationCell LineGenomicsHistone AcetyltransferasesHistone CodeHistonesNucleosomesRNARNA, MessengerTranscription Initiation SiteTranscriptomeTrypanosoma brucei bruceiHistone AcetyltransferasesHistonesNucleosomesRNARNA, Messenger

Identifiers

PMID32198348
PMCPMC7083915
OpenAlexW3011329694

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.