Evidence map›Paper›PMID 27365050›Full record

ArticleNucleic acids research2016

Chromatin structure-dependent conformations of the H1 CTD.

He Fang, Sijie Wei, Tae-Hee Lee, Jeffrey J Hayes

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Emergence of chromatin hierarchical loops from protein disorder and nucleosome asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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. 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

4 authors at 2 institutions in 1 country.

He FangDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA.
Sijie WeiDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
Tae-Hee LeeDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
Jeffrey J HayesDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA Jeffrey_Hayes@urmc.rochester.edu.
Pennsylvania State University · USUniversity of Rochester Medical Center · US

Funding

Histone Tall Interactions and Functions in ChromatinR01GM052426 · NIGMS · UNIVERSITY OF ROCHESTER · PI HAYES, JEFFREY J · 1995 to 2021
$6.2M
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 GM052426NIGMS NIH HHS R01 GM097286
6 · The paper itself

Abstract

Linker histones are an integral component of chromatin but how these proteins promote assembly of chromatin fibers and higher order structures and regulate gene expression remains an open question. Using Förster resonance energy transfer (FRET) approaches we find that association of a linker histone with oligonucleosomal arrays induces condensation of the intrinsically disordered H1 CTD in a manner consistent with adoption of a defined fold or ensemble of folds in the bound state. However, H1 CTD structure when bound to nucleosomes in arrays is distinct from that induced upon H1 association with mononucleosomes or bare double stranded DNA. Moreover, the H1 CTD becomes more condensed upon condensation of extended nucleosome arrays to the contacting zig-zag form found in moderate salts, but does not detectably change during folding to fully compacted chromatin fibers. We provide evidence that linker DNA conformation is a key determinant of H1 CTD structure and that constraints imposed by neighboring nucleosomes cause linker DNAs to adopt distinct trajectories in oligonucleosomes compared to H1-bound mononucleosomes. Finally, inter-molecular FRET between H1s within fully condensed nucleosome arrays suggests a regular spatial arrangement for the H1 CTD within the 30 nm chromatin fiber.

Indexed as

Nucleic Acid ConformationProtein ConformationAnimalsChromatinDNAFluorescence Resonance Energy TransferHistonesNucleosomesProtein BindingRecombinant ProteinsChromatinDNAHistonesNucleosomesRecombinant Proteins

Identifiers

PMID27365050
PMCPMC5100576
OpenAlexW2470377014

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.