Evidence map›Paper›PMID 21835779›Full record

ArticleNucleic acids research2011

From crystal and NMR structures, footprints and cryo-electron-micrographs to large and soft structures: nanoscale modeling of the nucleosomal stem.

Sam Meyer, Nils B Becker, Sajad Hussain Syed, Damien Goutte-Gattat, Manu Shubhdarshan Shukla, Jeffrey J Hayes, Dimitar Angelov, Jan Bednar, Stefan Dimitrov, Ralf Everaers

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. A DNA condensation code for linker histones.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Highly disordered histone H1-DNA model complexes and their condensates.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Linker histones: novel insights into structure-specific recognition of the nucleosome.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2017
    Review
  14. Review
  15. Linker Histone in Diseases.International journal of biological sciences · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. Linker histone H1 and protein-protein interactions.Biochimica et biophysica acta · 2016
    Review
  20. The chromatin fiber: multiscale problems and approaches.Current opinion in structural biology · 2015
    Review
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

10 authors at 7 institutions in 2 countries.

Sam MeyerLaboratoire de Physique and Centre Blaise Pascal, École Normale Supérieure de Lyon, Université de Lyon, CNRS UMR 5672, 46 allée d'Italie 69364 Lyon cedex 07, France. sam.meyer@ens-lyon.fr
Nils B Becker
Sajad Hussain Syed
Damien Goutte-Gattat
Manu Shubhdarshan Shukla
Jeffrey J Hayes
Dimitar Angelov
Jan Bednar
Stefan Dimitrov
Ralf Everaers
Centre National de la Recherche Scientifique · FRUniversité Joseph Fourier · FRÉcole Normale Supérieure de Lyon · FRInstitut pour l'avancée des biosciences · FRLaboratoire Interdisciplinaire de Physique · FRUniversité Claude Bernard Lyon 1 · FRUniversité Grenoble Alpes · FR

Funding

Histone Tall Interactions and Functions in ChromatinR01GM052426 · NIGMS · UNIVERSITY OF ROCHESTER · PI HAYES, JEFFREY J · 1995 to 2021
$6.2M
NIGMS NIH HHS R01 GM052426
6 · The paper itself

Abstract

The interaction of histone H1 with linker DNA results in the formation of the nucleosomal stem structure, with considerable influence on chromatin organization. In a recent paper [Syed,S.H., Goutte-Gattat,D., Becker,N., Meyer,S., Shukla,M.S., Hayes,J.J., Everaers,R., Angelov,D., Bednar,J. and Dimitrov,S. (2010) Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome. Proc. Natl Acad. Sci. USA, 107, 9620-9625], we published results of biochemical footprinting and cryo-electron-micrographs of reconstituted mono-, di- and tri-nucleosomes, for H1 variants with different lengths of the cationic C-terminus. Here, we present a detailed account of the analysis of the experimental data and we include thermal fluctuations into our nano-scale model of the stem structure. By combining (i) crystal and NMR structures of the nucleosome core particle and H1, (ii) the known nano-scale structure and elasticity of DNA, (iii) footprinting information on the location of protected sites on the DNA backbone and (iv) cryo-electron micrographs of reconstituted tri-nucleosomes, we arrive at a description of a polymorphic, hierarchically organized stem with a typical length of 20 ± 2 base pairs. A comparison to linker conformations inferred for poly-601 fibers with different linker lengths suggests, that intra-stem interactions stabilize and facilitate the formation of dense chromatin fibers.

Indexed as

Models, MolecularBiomechanical PhenomenaCryoelectron MicroscopyCrystallography, X-RayDNAHistonesNuclear Magnetic Resonance, BiomolecularNucleosomesProtein FootprintingDNAHistonesNucleosomes

Identifiers

PMID21835779
PMCPMC3241633
OpenAlexW1968302366

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.