Evidence map›Paper›PMID 24906881›Full record

ArticleNucleic acids research2014

Dynamic condensation of linker histone C-terminal domain regulates chromatin structure.

Antoni Luque, Rosana Collepardo-Guevara, Sergei Grigoryev, Tamar Schlick

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 79 citations in OpenAlex.

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  15. Regulation of Chromatin Architecture by Transcription Factor Binding.bioRxiv : the preprint server for biology · 2023
    Article
  16. Epigenetics · 2023
    Review
  17. Article
  18. Article
  19. Genome modeling: From chromatin fibers to genes.Current opinion in structural biology · 2023
    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 4 institutions in 2 countries.

Antoni LuqueDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, USA.
Rosana Collepardo-GuevaraUniversity of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK.
Sergei GrigoryevDepartment of Biochemistry and Molecular Biology, Penn State University College of Medicine, Hershey, PA 17033, USA.
Tamar SchlickDepartment of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, USA Courant Institute of Mathematical Sciences, New York University, 251 Mercer Street, New York, NY 10012, USA schlick@nyu.edu.
Courant Institute of Mathematical Sciences · USNew York University · USPennsylvania State University · USUniversity of Cambridge · GB

Funding

Modeling Chromatin Organization and FunctionR01GM055164 · NIGMS · NEW YORK UNIVERSITY · PI SCHLICK, TAMAR · 1998 to 2015
$2.6M
6 · The paper itself

Abstract

The basic and intrinsically disordered C-terminal domain (CTD) of the linker histone (LH) is essential for chromatin compaction. However, its conformation upon nucleosome binding and its impact on chromatin organization remain unknown. Our mesoscale chromatin model with a flexible LH CTD captures a dynamic, salt-dependent condensation mechanism driven by charge neutralization between the LH and linker DNA. Namely, at low salt concentration, CTD condenses, but LH only interacts with the nucleosome and one linker DNA, resulting in a semi-open nucleosome configuration; at higher salt, LH interacts with the nucleosome and two linker DNAs, promoting stem formation and chromatin compaction. CTD charge reduction unfolds the domain and decondenses chromatin, a mechanism in consonance with reduced counterion screening in vitro and phosphorylated LH in vivo. Divalent ions counteract this decondensation effect by maintaining nucleosome stems and expelling the CTDs to the fiber exterior. Additionally, we explain that the CTD folding depends on the chromatin fiber size, and we show that the asymmetric structure of the LH globular head is responsible for the uneven interaction observed between the LH and the linker DNAs. All these mechanisms may impact epigenetic regulation and higher levels of chromatin folding.

Indexed as

ChromatinHistonesMagnesiumModels, MolecularNucleosomesProtein Structure, TertiaryChromatinHistonesMagnesiumNucleosomes

Identifiers

PMID24906881
PMCPMC4081093
OpenAlexW2100955698

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.