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 language | English (US) |
|---|---|
| Pages (from-to) | 760-768 |
| Number of pages | 9 |
| Journal | Journal of Nutritional Biochemistry |
| Volume | 18 |
| Issue number | 11 |
| DOIs | |
| State | Published - 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