Evidence map›Paper›PMID 26575591›Full record

ArticleThe journal of physical chemistry. B2015

Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome.

Jongseong Kim, Jaehyoun Lee, Tae-Hee Lee

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Mapping Allosteric Communication in the Nucleosome with Conditional Activity.Journal of chemical information and modeling · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Physical Chemistry of Epigenetics: Single-Molecule Investigations.The journal of physical chemistry. B · 2019
    Review
  20. Article
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

3 authors at 1 institution in 1 country.

Jongseong KimDepartment of Chemistry, Eberly College of Science, The Pennsylvania State University , University Park, Pennsylvania, 16802, United States.
Jaehyoun LeeDepartment of Chemistry, Eberly College of Science, The Pennsylvania State University , University Park, Pennsylvania, 16802, United States.
Tae-Hee LeeDepartment of Chemistry, Eberly College of Science, The Pennsylvania State University , University Park, Pennsylvania, 16802, United States.
Pennsylvania State University · US

Funding

Dynamics of nucleosome assembly/disassembly affected by chromatin modificationsR01GM097286 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI LEE, TAE-HEE · 2011 to 2015
$1.4M
NIGMS NIH HHS GM097286NIGMS NIH HHS R01 GM097286
6 · The paper itself

Abstract

The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit.

Indexed as

Molecular Dynamics SimulationAcetylationAnimalsDNAFluorescence Resonance Energy TransferHumansLysineModels, MolecularNucleosomesXenopus laevisDNALysineNucleosomes

Identifiers

PMID26575591
PMCPMC5436045
OpenAlexW2300065908

What OpenQuestion holds

Textmetadata
LicenceTDM
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.