K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells.
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 (gamma-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.
Camporeale
Gabriela
G
Department of Nutrition and Health Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583-0806, USA.
Oommen
Anna M
AM
Griffin
Jacob B
JB
Sarath
Gautam
G
Zempleni
Janos
J
D019921:Biotinylation; D002471:Cell Transformation, Neoplastic; D002822:Choriocarcinoma; D047369:Chromatin Immunoprecipitation; D006570:Heterochromatin / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D019169:Jurkat Cells; D008239:Lysine / Q000378:metabolism*; D034741:RNA, Small Interfering; D014407:Tumor Cells, Cultured
D006570:Heterochromatin; D006657:Histones; D034741:RNA, Small Interfering; D008239:Lysine