Evidence map›Paper›PMID 19812216›Full record

ArticleThe Journal of nutrition2009

Repression of transposable elements by histone biotinylation.

Janos Zempleni, Yap Ching Chew, Baolong Bao, Valerie Pestinger, Subhashinee S K Wijeratne

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of nutrition, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Rad6 Regulates Conidiation by Affecting the Biotin Metabolism inJournal of fungi (Basel, Switzerland) · 2024
    Article
  4. Article
  5. Diversity ofAnimals : an open access journal from MDPI · 2022
    Article
  6. Transposable Elements and Stress in Vertebrates: An Overview.International journal of molecular sciences · 2021
    Review
  7. Omics Insights into Animal Resilience and Stress Factors.Animals : an open access journal from MDPI · 2020
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Epigenetics: A New Bridge between Nutrition and Health.Advances in nutrition (Bethesda, Md.) · 2010
    Article
  13. Article
  14. 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

5 authors at 1 institution in 1 country.

Janos ZempleniDepartment of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583, USA. jzempleni2@unl.edu
Yap Ching Chew
Baolong Bao
Valerie Pestinger
Subhashinee S K Wijeratne
University of Nebraska–Lincoln · US

Funding

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
Epigenetic effects of biotin on activation of endogenous viral sequencesR21ES015206 · NIEHS · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2006 to 2007
$396k
NIDDK NIH HHS DK063945NIDDK NIH HHS DK077816NIDDK NIH HHS DK082476NIEHS NIH HHS ES015206
6 · The paper itself

Abstract

Transposable elements constitute >40% of the human genome; transposition of these elements increases genome instability and cancer risk. Epigenetic mechanisms are important for transcriptional repression of retrotransposons, thereby preventing transposition events. Binding of biotin to histones, mediated by holocarboxylase synthetase (HCS), is a novel histone mark that plays a role in gene regulation. Here, we review recent findings that biotinylation of lysine-12 in histone H4 (H4K12bio) is an epigenetic mechanism to repress long terminal repeat (LTR) retrotransposons in human and mouse cell lines, primary cells from human adults, and in Drosophila melanogaster. Further, evidence is summarized that supports a causal relationship between the repression of LTR in H4K12bio-depleted cells and increased production of viral particles, increased frequency of retrotransposition events, and increased frequency of chromosomal abnormalities in mammals and Drosophila. Although HCS interacts physically with histones H3 and H4, the mechanism responsible for targeting HCS to retrotransposons to mediate histone biotinylation is uncertain. We hypothesize that HCS binds specifically to genomic regions rich in methylated cytosines and catalyzes increased biotinylation of histone H4 at lysine-12. Further, we hypothesize that this biotinylation promotes the subsequent dimethylation of lysine-9 in histone H3, resulting in an overall synergistic effect of 3 diet-dependent covalent modifications of histones in the repression of LTR.

Indexed as

Amino Acid SequenceAnimalsBiotinBiotinylationChromosome AberrationsDNA Transposable ElementsDrosophila melanogasterFolic AcidGenome, HumanHistonesHumansMiceMolecular Sequence DataTerminal Repeat SequencesBiotinDNA Transposable ElementsFolic AcidHistones

Identifiers

PMID19812216
PMCPMC2777482
OpenAlexW2108577922

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.