Evidence map›Paper›PMID 28128545›Full record

ArticleBiochemistry2017

Single-Molecule Investigations on Histone H2A-H2B Dynamics in the Nucleosome.

Jaehyoun Lee, Tae-Hee Lee

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2017. 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
1.7field-weighted citation impact, top 16% 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, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. DNA curtains to visualize chromatin interactions.Methods (San Diego, Calif.) · 2023
    Article
  8. Assignment of structural transitions during mechanical unwrapping of nucleosomes and their disassembly products.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Multicolor single-molecule FRET for DNA and RNA processes.Current opinion in structural biology · 2021
    Review
  11. Article
  12. Nucleosome Assembly and DisassemblyFrontiers in cell and developmental biology · 2021
    Article
  13. Article
  14. Article
  15. Physical Chemistry of Epigenetics: Single-Molecule Investigations.The journal of physical chemistry. B · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Livin Regulates H2A.XFrontiers in oncology · 2019
    Article
  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

2 authors at 1 institution in 1 country.

Jaehyoun LeeDepartment of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Tae-Hee LeeDepartment of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.ORCID 0000-0003-2034-6394
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 R01 GM097286
6 · The paper itself

Abstract

Nucleosomes impose physical barriers to DNA-templated processes, playing important roles in eukaryotic gene regulation. DNA is packaged into nucleosomes by histone proteins mainly through strong electrostatic interactions that can be modulated by various post-translational histone modifications. Investigating the dynamics of histone dissociation from the nucleosome and how it is altered upon histone modifications is important for understanding eukaryotic gene regulation mechanisms. In particular, histone H2A-H2B dimer displacement in the nucleosome is one of the most important and earliest steps of histone dissociation. Two conflicting hypotheses on the requirement for dimer displacement are that nucleosomal DNA needs to be unwrapped before a dimer can displace and that a dimer can displace without DNA unwrapping. In order to test the hypotheses, we employed three-color single-molecule FRET and monitored in a time-resolved manner the early kinetics of H2A-H2B dimer dissociation triggered by high salt concentration and by histone chaperone Nap1. The results reveal that dimer displacement requires DNA unwrapping in the vast majority of the nucleosomes in the salt-induced case, while dimer displacement precedes DNA unwrapping in >60% of the nucleosomes in the Nap1-mediated case. We also found that acetylation at histone H4K16 or H3K56 affects the kinetics of Nap1-mediated dimer dissociation and facilitates the process both kinetically and thermodynamically. On the basis of these results, we suggest a mechanism by which histone chaperone facilitates H2A-H2B dimer displacement from the histone core without requiring another factor to unwrap the nucleosomal DNA.

Indexed as

AcetylationDNAFluorescence Resonance Energy TransferHistonesMarkov ChainsNucleosome Assembly Protein 1NucleosomesProtein MultimerizationSaccharomyces cerevisiae ProteinsSingle Molecule ImagingThermodynamicsXenopus ProteinsDNAHistonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1NucleosomesSaccharomyces cerevisiae ProteinsXenopus Proteins

Identifiers

PMID28128545
PMCPMC5436051
OpenAlexW2581069230

What OpenQuestion holds

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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.