Biological functions of biotinylated histones

Nagarama Kothapalli, Gabriela Camporeale, Alice Kueh, Yap C. Chew, Anna M. Oommen, Jacob B. Griffin, Janos Zempleni

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


Histones H1, H2A, H2B, H3 and H4 are DNA-binding proteins that mediate the folding of DNA into chromatin. Various posttranslational modifications of histones regulate processes such as transcription, replication and repair of DNA. Recently, a novel posttranslational modification has been identified: covalent binding of the vitamin biotin to lysine residues in histones, mediated by biotinidase and holocarboxylase synthetase. Here we describe a novel peptide-based technique, which was used to identify eight distinct biotinylation sites in histones H2A, H3 and H4. Biotinylation site-specific antibodies were generated to investigate biological functions of histone biotinylation. Evidence was provided that biotinylation of histones plays a role in cell proliferation, gene silencing and cellular response to DNA damage.

Original languageEnglish (US)
Pages (from-to)446-448
Number of pages3
JournalJournal of Nutritional Biochemistry
Issue number7
StatePublished - Jul 2005


  • Biotin
  • Chromatin
  • DNA damage
  • Epigenetics
  • Histones
  • Human

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Biology
  • Nutrition and Dietetics
  • Clinical Biochemistry

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