Evidence map›Paper›PMID 31956896›Full record

ArticleNucleic acids research2020

Dynamics of the nucleosomal histone H3 N-terminal tail revealed by high precision single-molecule FRET.

Kathrin Lehmann, Suren Felekyan, Ralf Kühnemuth, Mykola Dimura, Katalin Tóth, Claus A M Seidel, Jörg Langowski

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 46 citations in OpenAlex.

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  9. Construction of Histone-Protein Complex Structures by Peptide Growing.International journal of molecular sciences · 2023
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  14. Arginine anchor points govern H3 tail dynamics.Frontiers in molecular biosciences · 2023
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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

7 authors at 2 institutions in 1 country.

Kathrin LehmannDivision Biophysics of Macromolecules, German Cancer Research Center, Heidelberg D-69120, Germany.
Suren FelekyanLehrstuhl für Molekulare Physikalische Chemie, Heinrich-Heine-Universität, Düsseldorf D-40225, Germany.
Ralf KühnemuthLehrstuhl für Molekulare Physikalische Chemie, Heinrich-Heine-Universität, Düsseldorf D-40225, Germany.
Mykola DimuraLehrstuhl für Molekulare Physikalische Chemie, Heinrich-Heine-Universität, Düsseldorf D-40225, Germany.
Katalin TóthDivision Biophysics of Macromolecules, German Cancer Research Center, Heidelberg D-69120, Germany.
Claus A M SeidelLehrstuhl für Molekulare Physikalische Chemie, Heinrich-Heine-Universität, Düsseldorf D-40225, Germany.
Jörg LangowskiDivision Biophysics of Macromolecules, German Cancer Research Center, Heidelberg D-69120, Germany.
Heinrich Heine University Düsseldorf · DEGerman Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin compaction and gene accessibility are orchestrated by assembly and disassembly of nucleosomes. Although the disassembly process was widely studied, little is known about the structure and dynamics of the disordered histone tails, which play a pivotal role for nucleosome integrity. This is a gap filling experimental FRET study from the perspective of the histone H3 N-terminal tail (H3NtT) of reconstituted mononucleosomes. By systematic variation of the labeling positions we monitored the motions of the H3NtT relative to the dyad axis and linker DNA. Single-molecule FRET unveiled that H3NtTs do not diffuse freely but follow the DNA motions with multiple interaction modes with certain permitted dynamic transitions in the μs to ms time range. We also demonstrate that the H3NtT can allosterically sense charge-modifying mutations within the histone core (helix α3 of histone H2A (R81E/R88E)) resulting in increased dynamic transitions and lower rate constants. Those results complement our earlier model on the NaCl induced nucleosome disassembly as changes in H3NtT configurations coincide with two major steps: unwrapping of one linker DNA and weakening of the internal DNA - histone interactions on the other side. This emphasizes the contribution of the H3NtT to the fine-tuned equilibrium between overall nucleosome stability and DNA accessibility.

Indexed as

AnimalsChromatinChromatin Assembly and DisassemblyDNAFluorescence Resonance Energy TransferHistonesMutationNanotechnologyNucleic Acid ConformationNucleosomesProtein BindingSingle Molecule ImagingXenopus laevisChromatinDNAHistonesNucleosomes

Identifiers

PMID31956896
PMCPMC7026643
OpenAlexW3002867854

What OpenQuestion holds

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LicenceCC BY-NC
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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.