Evidence map›Paper›PMID 32097625›Full record

ArticleBiophysical journal2020

Minimal Cylinder Analysis Reveals the Mechanical Properties of Oncogenic Nucleosomes.

Mary Pitman, Yamini Dalal, Garegin A Papoian

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Genome modeling: From chromatin fibers to genes.Current opinion in structural biology · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Intrinsic elasticity of nucleosomes is encoded by histone variants and calibrated by their binding partners.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

3 authors at 2 institutions in 1 country.

Mary PitmanLaboratory of Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland; Department of Chemistry and Biochemistry, Institute for Physical Science and Technology, University of Maryland, College Park, Maryland.
Yamini DalalLaboratory of Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland. Electronic address: dalaly@mail.nih.gov.
Garegin A PapoianDepartment of Chemistry and Biochemistry, Institute for Physical Science and Technology, University of Maryland, College Park, Maryland. Electronic address: gpapoian@umd.edu.
National Cancer Institute · USUniversity of Maryland, College Park · US

Funding

Role of histone variants in aging and cancerZIABC011206 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DALAL, YAMINI P · 2009 to 2025
$10.4M
6 · The paper itself

Abstract

Histone variants regulate replication, transcription, DNA damage repair, and chromosome segregation. Though widely accepted as a paradigm, it has not been rigorously demonstrated that histone variants encode unique mechanical properties. Here, we present a new theoretical approach called minimal cylinder analysis that uses strain fluctuations to determine the Young's modulus of nucleosomes from all-atom molecular dynamics simulations. Recently, we validated this computational tool against in vitro single-molecule nanoindentation of histone variant nucleosomes. In this report, we further extend minimal cylinder analysis to study the biophysical properties of hybrid nucleosomes that are known to exist in human cancer cells and contain H3 histone variants CENP-A and H3.3. Here, we report that the heterotypic nucleosome has an intermediate elasticity (8.5 ± 0.5 MPa) compared to CENP-A (6.2 ± 0.4 MPa) and H3 (9.8 ± 0.7 MPa) and that the dynamics of both canonical and CENP-A nucleosomes are preserved and partitioned across the nucleosome pseudodyad. Furthermore, we investigate the mechanism by which the elasticity of these heterotypic nucleosomes augments cryptic binding surfaces. From these analyses, we predict that the heterotypic nucleosome is permissive to the binding of one copy of the kinetochore protein CENP-C while still retaining a closed DNA end configuration required for linker histone H1 to bind. We discuss that the ectopic deposition of CENP-A in cancer by H3.3 chaperones HIRA and DAXX may fortuitously result in hybrid nucleosome formation. Using these results, we propose biological outcomes that might arise when such heterotypic nucleosomes occupy large regions of the genome.

Indexed as

KinetochoresNucleosomesAutoantigensCentromereCentromere Protein AChromosome SegregationDNAHumansAutoantigensCentromere Protein ADNANucleosomes

Identifiers

PMID32097625
PMCPMC7203005
OpenAlexW3005551104

What Socratic 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 Socratic graph.