Evidence map›Paper›PMID 34057467›Full record

ArticleNucleic acids research2021

Cooperative DNA looping by PRC2 complexes.

Xingcheng Lin, Rachel Leicher, Shixin Liu, Bin Zhang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

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  20. Phase Separation and Correlated Motions in Motorized Genome.The journal of physical chemistry. B · 2022
    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 3 institutions in 1 country.

Xingcheng LinDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-9378-6174
Rachel LeicherLaboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY 10065, USA.
Shixin LiuLaboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY 10065, USA.
Bin ZhangDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-3685-7503
Massachusetts Institute of Technology · USRockefeller University · USTri-Institutional PhD Program in Chemical Biology · US

Funding

Probing and Perturbing Transcriptional Condensates with Multiscale Modeling and Deep LearningR35GM133580 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Bin Zhang · 2019 to 2026
$3.1M
Probing Symmetry Breaking in Epigenetic Inheritance: From Single Molecules to Systems BiologyDP2HG010510 · NHGRI · ROCKEFELLER UNIVERSITY · PI LIU, SHIXIN · 2018 to 2018
$2.5M
NHGRI NIH HHS DP2 HG010510NIGMS NIH HHS R35 GM133580
6 · The paper itself

Abstract

Polycomb repressive complex 2 (PRC2) is an essential protein complex that silences gene expression via post-translational modifications of chromatin. This paper combined homology modeling, atomistic and coarse-grained molecular dynamics simulations, and single-molecule force spectroscopy experiments to characterize both its full-length structure and PRC2-DNA interactions. Using free energy calculations with a newly parameterized protein-DNA force field, we studied a total of three potential PRC2 conformations and their impact on DNA binding and bending. Consistent with cryo-EM studies, we found that EZH2, a core subunit of PRC2, provides the primary interface for DNA binding, and its curved surface can induce DNA bending. Our simulations also predicted the C2 domain of the SUZ12 subunit to contact DNA. Multiple PRC2 complexes bind with DNA cooperatively via allosteric communication through the DNA, leading to a hairpin-like looped configuration. Single-molecule experiments support PRC2-mediated DNA looping and the role of AEBP2 in regulating such loop formation. The impact of AEBP2 can be partly understood from its association with the C2 domain, blocking C2 from DNA binding. Our study suggests that accessory proteins may regulate the genomic location of PRC2 by interfering with its DNA interactions.

Indexed as

DNAMolecular Dynamics SimulationNucleic Acid ConformationPolycomb Repressive Complex 2Protein BindingProtein ConformationDNAPolycomb Repressive Complex 2

Identifiers

PMID34057467
PMCPMC8216278
OpenAlexW3164690700

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.