Evidence map›Paper›PMID 34108453›Full record

ArticleNature communications2021

Site-specific ubiquitylation acts as a regulator of linker histone H1.

Eva Höllmüller, Simon Geigges, Marie L Niedermeier, Kai-Michael Kammer, Simon M Kienle, Daniel Rösner, Martin Scheffner, Andreas Marx, Florian Stengel

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  6. Photocatalytic Diselenide Contraction as a Tool for Site-Selective Isosteric Ubiquitylation.Journal of peptide science : an official publication of the European Peptide Society · 2025
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  15. Review
  16. Article
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  19. Article
  20. Site-specific ubiquitination: Deconstructing the degradation tag.Current opinion in structural biology · 2022
    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

9 authors at 1 institution in 1 country.

Eva Höllmüller *Department of Chemistry, University of Konstanz, Konstanz, Germany.
Simon Geigges *Department of Chemistry, University of Konstanz, Konstanz, Germany.
Marie L NiedermeierDepartment of Biology, University of Konstanz, Konstanz, Germany.
Kai-Michael KammerDepartment of Biology, University of Konstanz, Konstanz, Germany.
Simon M KienleDepartment of Biology, University of Konstanz, Konstanz, Germany.
Daniel RösnerDepartment of Chemistry, University of Konstanz, Konstanz, Germany.
Martin ScheffnerDepartment of Biology, University of Konstanz, Konstanz, Germany. martin.scheffner@uni-konstanz.de.ORCID 0000-0003-2229-0128
Andreas MarxDepartment of Chemistry, University of Konstanz, Konstanz, Germany. andreas.marx@uni-konstanz.de.ORCID 0000-0002-6471-3689
Florian StengelDepartment of Biology, University of Konstanz, Konstanz, Germany. florian.stengel@uni-konstanz.de.ORCID 0000-0003-1447-4509
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Decoding the role of histone posttranslational modifications (PTMs) is key to understand the fundamental process of epigenetic regulation. This is well studied for PTMs of core histones but not for linker histone H1 in general and its ubiquitylation in particular due to a lack of proper tools. Here, we report on the chemical synthesis of site-specifically mono-ubiquitylated H1.2 and identify its ubiquitin-dependent interactome on a proteome-wide scale. We show that site-specific ubiquitylation of H1 at position K64 modulates interactions with deubiquitylating enzymes and the deacetylase SIRT1. Moreover, it affects H1-dependent chromatosome assembly and phase separation resulting in a more open chromatosome conformation generally associated with a transcriptionally active chromatin state. In summary, we propose that site-specific ubiquitylation plays a general regulatory role for linker histone H1.

Indexed as

ChromatinDeubiquitinating EnzymesEpigenesis, GeneticHistonesHumansNucleosomesProtein BindingProtein Interaction MapsSirtuin 1UbiquitinUbiquitinationChromatinDeubiquitinating EnzymesH1-2 protein, humanHistonesNucleosomesSIRT1 protein, humanSirtuin 1Ubiquitin

Identifiers

PMID34108453
PMCPMC8190259
OpenAlexW3171072400

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.