A novel, enigmatic histone modification: Biotinylation of histones by holocarboxylase synthetase

Yousef I. Hassan, Janos Zempleni

Research output: Contribution to journalReview article

32 Citations (Scopus)

Abstract

Holocarboxylase synthetase catalyzes the covalent binding of biotin to histones in humans and other eukaryotes. Eleven biotinylation sites have been identified in histones H2A, H3, and H4. K12-biotinylated histone H4 is enriched in heterochromatin, repeat regions, and plays a role in gene repression. About 30% of the histone H4 molecules are biotinylated at K12 in histone H4 in human fibroblast telomeres. The abundance of biotinylated histones at distinct genomic loci depends on biotin availability. Decreased histone biotinylation decreases life span and stress resistance in Drosophila. Low enrichment of biotinylated histones at transposable elements impairs repression of these elements.

Original languageEnglish (US)
Pages (from-to)721-725
Number of pages5
JournalNutrition Reviews
Volume66
Issue number12
DOIs
StatePublished - Dec 1 2008

Fingerprint

Histone Code
Biotinylation
Histones
Biotin
holocarboxylase synthetases
DNA Transposable Elements
Heterochromatin
Telomere
Eukaryota
Psychological Stress
Drosophila
Fibroblasts

Keywords

  • Biotin
  • Chromatin
  • Epigenetics
  • Histones
  • Holocarboxylase synthetase

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Nutrition and Dietetics

Cite this

A novel, enigmatic histone modification : Biotinylation of histones by holocarboxylase synthetase. / Hassan, Yousef I.; Zempleni, Janos.

In: Nutrition Reviews, Vol. 66, No. 12, 01.12.2008, p. 721-725.

Research output: Contribution to journalReview article

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