Evidence map›Paper›PMID 21298003›Full record

ArticlePloS one2011

The role of histone H4 biotinylation in the structure of nucleosomes.

Nina A Filenko, Carol Kolar, John T West, S Abbie Smith, Yousef I Hassan, Gloria E O Borgstahl, Janos Zempleni, Yuri L Lyubchenko

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. PARP3 Affects Nucleosome Compaction Regulation.International journal of molecular sciences · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Sequence-dependent nucleosome nanoscale structure characterized by atomic force microscopy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  12. Article
  13. Article
  14. Imaging of DNA and Protein-DNA Complexes with Atomic Force Microscopy.Critical reviews in eukaryotic gene expression · 2016
    Review
  15. Review
  16. Chromatin imaging with time-lapse atomic force microscopy.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  17. Review
  18. Article
  19. Article
  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

8 authors at 3 institutions in 1 country.

Nina A FilenkoDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Carol Kolar
John T West
S Abbie Smith
Yousef I Hassan
Gloria E O Borgstahl
Janos Zempleni
Yuri L Lyubchenko
University of Nebraska Medical Center · USUniversity of Nebraska–Lincoln · USUniversity of Oklahoma Health Sciences Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
Vitamin-dependent modifications of histonesR01DK063945 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2004 to 2011
$2.3M
Biotin sensing and chromatin remodeling by holocarboxylase synthetaseR01DK077816 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2009 to 2011
$861k
Novel histone biotinylation sites and relationships to other epigenetic marksR21DK082476 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI CHANG, YIE-HWA, EISSENBERG, JOEL C · 2009 to 2010
$535k
NCI NIH HHS P30 CA036727NCI NIH HHS P30CA036727NIDDK NIH HHS DK063945NIDDK NIH HHS DK077816NIDDK NIH HHS DK082476NIDDK NIH HHS R01 DK063945NIDDK NIH HHS R01 DK077816NIDDK NIH HHS R21 DK082476
6 · The paper itself

Abstract

backgroundPost-translational modifications of histones play important roles in regulating nucleosome structure and gene transcription. It has been shown that biotinylation of histone H4 at lysine-12 in histone H4 (K12Bio-H4) is associated with repression of a number of genes. We hypothesized that biotinylation modifies the physical structure of nucleosomes, and that biotin-induced conformational changes contribute to gene silencing associated with histone biotinylation. METHODOLOGY/PRINCIPAL

findingsTo test this hypothesis we used atomic force microscopy to directly analyze structures of nucleosomes formed with biotin-modified and non-modified H4. The analysis of the AFM images revealed a 13% increase in the length of DNA wrapped around the histone core in nucleosomes with biotinylated H4. This statistically significant (p<0.001) difference between native and biotinylated nucleosomes corresponds to adding approximately 20 bp to the classical 147 bp length of nucleosomal DNA. CONCLUSIONS/SIGNIFICANCE: The increase in nucleosomal DNA length is predicted to stabilize the association of DNA with histones and therefore to prevent nucleosomes from unwrapping. This provides a mechanistic explanation for the gene silencing associated with K12Bio-H4. The proposed single-molecule AFM approach will be instrumental for studying the effects of various epigenetic modifications of nucleosomes, in addition to biotinylation.

Indexed as

AnimalsBiotinylationDNAGene SilencingHistonesMicroscopy, Atomic ForceNucleic Acid ConformationNucleosomesProtein Processing, Post-TranslationalXenopus ProteinsDNAHistonesNucleosomesXenopus Proteins

Identifiers

PMID21298003
PMCPMC3029316
OpenAlexW2061163762

What OpenQuestion holds

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Registered trials

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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.