K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells

Gabriela Camporeale, Anna M. Oommen, Jacob B. Griffin, Gautam Sarath, Janos Zempleni

Research output: Contribution to journalArticle

57 Scopus citations

Abstract

Covalent modifications of histones play crucial roles in chromatin structure and genomic stability. Recently, we reported a novel modification of histones: biotinylation of lysine residues. Here we provide evidence that K12-biotinylated histone H4 (K12Bio H4) maps specifically to both heterochromatin (alpha satellite repeats in pericentromeric regions) and transcriptionally repressed chromatin (γ-G globin and interleukin-2) in human lymphoblastoma cells. The abundance of K12Bio H4 in these regions was similar to that of K9-dimethylated histone H3, a known marker for heterochromatin. Likewise, K8-biotinylated histone H4 (K8Bio H4) mapped to heterochromatin, but the relative enrichment was smaller compared with K12Bio H4. Stimulation of interleukin-2 transcriptional activity with phorbol-12-myristate-13-acetate and phytohemagglutinin caused a rapid depletion of K12Bio H4 in the gene promoter. These data are consistent with a novel role for biotin in chromatin structure and transcriptional activity of genes.

Original languageEnglish (US)
Pages (from-to)760-768
Number of pages9
JournalJournal of Nutritional Biochemistry
Volume18
Issue number11
DOIs
StatePublished - Nov 2007

Keywords

  • Biotin
  • Chromatin immunoprecipitation
  • Heterochromatin
  • Histone
  • Human

ASJC Scopus subject areas

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

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