期刊
JOURNAL OF NUTRITIONAL BIOCHEMISTRY
卷 18, 期 11, 页码 760-768出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jnutbio.2006.12.014
关键词
biotin; chromatin immunoprecipitation; heterochromatin; histone; human
资金
- NCRR NIH HHS [1 P20 RR16469, P20 RR016469] Funding Source: Medline
- NIDDK NIH HHS [R01 DK063945-03, DK 63945, R01 DK063945] Funding Source: Medline
- NIEHS NIH HHS [R21 ES015206, R21 ES015206-01] Funding Source: Medline
Covalent modifications of histones play crucial roles in chromatin structure and genomic stability. Recently, we reported a novel modification of histories: 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 lymphoblastorna 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 interieukin-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. (C) 2007 Elsevier Inc. All rights reserved.
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