Evidence map›Paper›PMID 32165536›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Emergence of chromatin hierarchical loops from protein disorder and nucleosome asymmetry.

Akshay Sridhar, Stephen E Farr, Guillem Portella, Tamar Schlick, Modesto Orozco, Rosana Collepardo-Guevara

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-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

26 citing papers in PubMed, 47 citations in OpenAlex.

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  15. Genome modeling: From chromatin fibers to genes.Current opinion in structural biology · 2023
    Review
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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

6 authors at 3 institutions in 4 countries.

Akshay SridharMaxwell Centre, Cavendish Laboratory, University of Cambridge, CB3 0HE Cambridge, United Kingdom.
Stephen E FarrMaxwell Centre, Cavendish Laboratory, University of Cambridge, CB3 0HE Cambridge, United Kingdom.
Guillem PortellaChemistry Department, University of Cambridge, CB2 1EW Cambridge, United Kingdom.
Tamar SchlickDepartment of Chemistry, New York University, New York, NY 10003.ORCID 0000-0002-2392-2062
Modesto OrozcoInstitute for Research in Biomedicine, The Barcelona Institute of Science and Technology, 08028 Barcelona, Spain.
Rosana Collepardo-GuevaraMaxwell Centre, Cavendish Laboratory, University of Cambridge, CB3 0HE Cambridge, United Kingdom; rc597@cam.ac.uk.ORCID 0000-0003-1781-7351
University of Cambridge · GBInstitute for Research in Biomedicine · ESNew York University Shanghai · CN

Funding

Bridging Disparate Structural/Functional Scales: Multiscale Modeling of the Chromatin Fiber and RNA Tertiary StructuresR35GM122562 · NIGMS · NEW YORK UNIVERSITY · PI Tamar Schlick · 2017 to 2026
$4.6M
Modeling Chromatin Organization and FunctionR01GM055164 · NIGMS · NEW YORK UNIVERSITY · PI SCHLICK, TAMAR · 1998 to 2015
$2.6M
NIGMS NIH HHS R01 GM055164NIGMS NIH HHS R35 GM122562Wellcome TrustWellcome Trust 099232/Z/12/Z
6 · The paper itself

Abstract

Protein flexibility and disorder is emerging as a crucial modulator of chromatin structure. Histone tail disorder enables transient binding of different molecules to the nucleosomes, thereby promoting heterogeneous and dynamic internucleosome interactions and making possible recruitment of a wide-range of regulatory and remodeling proteins. On the basis of extensive multiscale modeling we reveal the importance of linker histone H1 protein disorder for chromatin hierarchical looping. Our multiscale approach bridges microsecond-long bias-exchange metadynamics molecular dynamics simulations of atomistic 211-bp nucleosomes with coarse-grained Monte Carlo simulations of 100-nucleosome systems. We show that the long C-terminal domain (CTD) of H1-a ubiquitous nucleosome-binding protein-remains disordered when bound to the nucleosome. Notably, such CTD disorder leads to an asymmetric and dynamical nucleosome conformation that promotes chromatin structural flexibility and establishes long-range hierarchical loops. Furthermore, the degree of condensation and flexibility of H1 can be fine-tuned, explaining chromosomal differences of interphase versus metaphase states that correspond to partial and hyperphosphorylated H1, respectively. This important role of H1 protein disorder in large-scale chromatin organization has a wide range of biological implications.

Indexed as

AnimalsChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistonesHumansMetaphaseModels, MolecularNucleic Acid ConformationNucleosomesProtein BindingChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistonesNucleosomeschromatin polymorphismCTD of H1H1-nucleosome bindingnucleosome asymmetryprotein disorder

Identifiers

PMID32165536
PMCPMC7132128
OpenAlexW3010849995

What OpenQuestion holds

Textmetadata
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.