The role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events

Janos Zempleni, Yong Li, Jing Xue, Elizabeth L. Cordonier

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Holocarboxylase synthetase (HLCS) -catalyzes the covalent binding of biotin to histones. Biotinylated histones are gene repression marks and are particularly enriched in long terminal repeats, telomeres and other repeat regions. The effects of HLCS in gene regulation are mediated by its physical interactions with chromatin proteins such as histone H3, DNMT1, MeCP2 and EHMT-1. It appears that histone biotinylation depends on prior methylation of cytosines. De-repression of long terminal repeats in biotin- or HLCS-deficient cell cultures and organisms is associated with genome instability.

Original languageEnglish (US)
Pages (from-to)892-894
Number of pages3
JournalEpigenetics
Volume6
Issue number7
DOIs
StatePublished - Jan 1 2011

Fingerprint

Biotinylation
Genomic Instability
Epigenomics
Histones
Methylation
Terminal Repeat Sequences
Cytosine
Telomere
Biotin
Genes
Chromatin
Cell Culture Techniques
holocarboxylase synthetases
Proteins

Keywords

  • Biotin
  • DNMT1
  • EHMT-1
  • Genome stability
  • Histone
  • Holocarboxylase synthetase
  • MeCP2
  • Methylation

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research

Cite this

The role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events. / Zempleni, Janos; Li, Yong; Xue, Jing; Cordonier, Elizabeth L.

In: Epigenetics, Vol. 6, No. 7, 01.01.2011, p. 892-894.

Research output: Contribution to journalArticle

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