Evidence map›Paper›PMID 26820416›Full record

ArticlePloS one2016

Histone H1 Variants in Arabidopsis Are Subject to Numerous Post-Translational Modifications, Both Conserved and Previously Unknown in Histones, Suggesting Complex Functions of H1 in Plants.

Maciej Kotliński, Kinga Rutowicz, Łukasz Kniżewski, Antoni Palusiński, Jacek Olędzki, Anna Fogtman, Tymon Rubel, Marta Koblowska, Michał Dadlez, Krzysztof Ginalski and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

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  17. Salicylic acid interferes with GFP fluorescence in vivo.Journal of experimental botany · 2017
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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

11 authors at 3 institutions in 1 country.

Maciej KotlińskiLaboratory of Systems Biology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Kinga RutowiczInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Łukasz KniżewskiLaboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Warsaw, Poland.
Antoni PalusińskiLaboratory of Systems Biology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Jacek OlędzkiInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Anna FogtmanInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Tymon RubelInstitute of Radioelectronic and Multimedia Technology, Warsaw University of Technology, Warsaw, Poland.
Marta KoblowskaLaboratory of Systems Biology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Michał DadlezInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Krzysztof GinalskiLaboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Warsaw, Poland.
Andrzej JerzmanowskiLaboratory of Systems Biology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLUniversity of Warsaw · PLWarsaw University of Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Linker histones (H1s) are conserved and ubiquitous structural components of eukaryotic chromatin. Multiple non-allelic variants of H1, which differ in their DNA/nucleosome binding properties, co-exist in animal and plant cells and have been implicated in the control of genetic programs during development and differentiation. Studies in mammals and Drosophila have revealed diverse post-translational modifications of H1s, most of which are of unknown function. So far, it is not known how this pattern compares with that of H1s from other major lineages of multicellular Eukaryotes. Here, we show that the two main H1variants of a model flowering plant Arabidopsis thaliana are subject to a rich and diverse array of post-translational modifications. The distribution of these modifications in the H1 molecule, especially in its globular domain (GH1), resembles that occurring in mammalian H1s, suggesting that their functional significance is likely to be conserved. While the majority of modifications detected in Arabidopsis H1s, including phosphorylation, acetylation, mono- and dimethylation, formylation, crotonylation and propionylation, have also been reported in H1s of other species, some others have not been previously identified in histones.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceArabidopsisArabidopsis ProteinsConserved SequenceHistonesMethylationModels, MolecularMolecular Sequence DataNucleosomesPhosphorylationProtein Structure, TertiaryArabidopsis ProteinsHistonesNucleosomes

Identifiers

PMID26820416
PMCPMC4731575
OpenAlexW2273656950

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.