Evidence map›Paper›PMID 21059934›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Tetrameric organization of vertebrate centromeric nucleosomes.

Emilios K Dimitriadis, Christian Weber, Rajbir K Gill, Stephan Diekmann, Yamini Dalal

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
20.7field-weighted citation impact, top 1% 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

67 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Review
  3. The dynamic centromere.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. 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
  14. Article
  15. Article
  16. Article
  17. Peering at Brain Polysomes with Atomic Force Microscopy.Journal of visualized experiments : JoVE · 2016
    Article
  18. Article
  19. Review
  20. Article

7 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 2 countries.

Emilios K DimitriadisScanning Probe Microscopy Unit, Biomedical Engineering and Physical Science Shared Resource, National Institute for Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892, USA.
Christian Weber
Rajbir K Gill
Stephan Diekmann
Yamini Dalal
Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DENational Institutes of Health · USNational Cancer Institute · US

Funding

Biomechanical properties of chromatin in cancer and normal cellsZIABC011207 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DALAL, YAMINI P · 2009 to 2025
$8.8M
Kinetochore Interaction with Centromere Chromatin in human cellsZIABC011209 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DALAL, YAMINI P · 2009 to 2025
$5.5M
Study on the Nature of the Centromeric NucleosomeZICEB000070 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI DIMITRIADIS, EMILIOS K · 2010 to 2012
$94k
Intramural NIH HHS ZIA BC011207
6 · The paper itself

Abstract

Mitosis ensures equal genome segregation in the eukaryotic lineage. This process is facilitated by microtubule attachment to each chromosome via its centromere. In centromeres, canonical histone H3 is replaced in nucleosomes by a centromere-specific histone H3 variant (CENH3), providing the unique epigenetic signature required for microtubule binding. Due to recent findings of alternative CENH3 nucleosomal forms in invertebrate centromeres, it has been debated whether the classical octameric nucleosomal arrangement of two copies of CENH3, H4, H2A, and H2B forms the basis of the vertebrate centromere. To address this question directly, we examined CENH3 [centromere protein A (CENP-A)] nucleosomal organization in human cells, using a combination of nucleosome component analysis, atomic force microscopy (AFM), and immunoelectron microscopy (immuno-EM). We report that native CENP-A nucleosomes contain centromeric alpha satellite DNA, have equimolar amounts of H2A, H2B, CENP-A, and H4, and bind kinetochore proteins. These nucleosomes, when measured by AFM, yield one-half the dimensions of canonical octameric nucleosomes. Using immuno-EM, we find that one copy of CENP-A, H2A, H2B, and H4 coexist in CENP-A nucleosomes, in which internal C-terminal domains are accessible. Our observations indicate that CENP-A nucleosomes are organized as asymmetric heterotypic tetramers, rather than canonical octamers. Such altered nucleosomes form a chromatin fiber with distinct folding characteristics, which we utilize to discriminate tetramers directly within bulk chromatin. We discuss implications of our observations in the context of universal epigenetic and mechanical requirements for functional centromeres.

Indexed as

AutoantigensCentromereCentromere Protein AChromosomal Proteins, Non-HistoneHumansMicroscopy, Atomic ForceMicroscopy, ImmunoelectronMicrotubulesMitosisNucleosomesAutoantigensCENPA protein, humanCentromere Protein AChromosomal Proteins, Non-HistoneNucleosomes

Identifiers

PMID21059934
PMCPMC2996678
OpenAlexW1970668361

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.