Evidence map›Paper›PMID 34086674›Full record

ArticlePLoS genetics2021

Crosstalk between H2A variant-specific modifications impacts vital cell functions.

Anna Schmücker, Bingkun Lei, Zdravko J Lorković, Matías Capella, Sigurd Braun, Pierre Bourguet, Olivier Mathieu, Karl Mechtler, Frédéric Berger

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

7 citing papers in PubMed, 21 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

9 authors at 4 institutions in 3 countries.

Anna SchmückerGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.ORCID 0000-0001-8409-761X
Bingkun LeiGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.ORCID 0000-0002-2773-1669
Zdravko J LorkovićGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.ORCID 0000-0002-3074-7258
Matías CapellaBiomedical Center, Department of Physiological Chemistry, Ludwig-Maximilians-University of Munich, Planegg-Martinsried, Germany.ORCID 0000-0003-4804-243X
Sigurd BraunBiomedical Center, Department of Physiological Chemistry, Ludwig-Maximilians-University of Munich, Planegg-Martinsried, Germany.ORCID 0000-0001-6399-8574
Pierre BourguetGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.ORCID 0000-0002-5019-4179
Olivier MathieuCNRS, Université Clermont Auvergne, Inserm, Génétique Reproduction et Développement, Clermont-Ferrand, France.ORCID 0000-0001-5302-1102
Karl MechtlerGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.ORCID 0000-0002-3392-9946
Frédéric BergerGregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.ORCID 0000-0002-3609-8260
Gregor Mendel Institute of Molecular Plant Biology · ATCentre National de la Recherche Scientifique · FRLudwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DE

Funding

Austrian Science Fund FWF P 26887Austrian Science Fund FWF P 28320Austrian Science Fund FWF P 30802Austrian Science Fund FWF P 32054Austrian Science Fund FWF TAI 304
6 · The paper itself

Abstract

Selection of C-terminal motifs participated in evolution of distinct histone H2A variants. Hybrid types of variants combining motifs from distinct H2A classes are extremely rare. This suggests that the proximity between the motif cases interferes with their function. We studied this question in flowering plants that evolved sporadically a hybrid H2A variant combining the SQ motif of H2A.X that participates in the DNA damage response with the KSPK motif of H2A.W that stabilizes heterochromatin. Our inventory of PTMs of H2A.W variants showed that in vivo the cell cycle-dependent kinase CDKA phosphorylates the KSPK motif of H2A.W but only in absence of an SQ motif. Phosphomimicry of KSPK prevented DNA damage response by the SQ motif of the hybrid H2A.W/X variant. In a synthetic yeast expressing the hybrid H2A.W/X variant, phosphorylation of KSPK prevented binding of the BRCT-domain protein Mdb1 to phosphorylated SQ and impaired response to DNA damage. Our findings illustrate that PTMs mediate interference between the function of H2A variant specific C-terminal motifs. Such interference could explain the mutual exclusion of motifs that led to evolution of H2A variants.

Indexed as

Gene Expression Regulation, PlantProtein Processing, Post-TranslationalAmino Acid SequenceArabidopsisArabidopsis ProteinsCell Culture TechniquesCell CycleChromosomal Proteins, Non-HistoneCyclin-Dependent KinasesDNA DamageEvolution, MolecularHeterochromatinHistonesPhosphorylationPlant CellsPlants, Genetically ModifiedArabidopsis ProteinsCDKA1 protein, ArabidopsisChromosomal Proteins, Non-HistoneCyclin-Dependent KinasesHeterochromatinHistonesMdb1 protein, S pombeProtein IsoformsSchizosaccharomyces pombe Proteins

Identifiers

PMID34086674
PMCPMC8208582
OpenAlexW3164704139

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.