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J. Biol. Chem., Vol. 276, Issue 44, 40373-40376, November 2, 2001

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ACCELERATED PUBLICATION
CCAAT/Enhancer-binding Protein  Alters Histone H3 Acetylation at Large Subnuclear Domains^*

Wan-Hui Zhang^§, Roopali Srihari^§, Richard N. Day^¶, and Fred Schaufele

From the  Metabolic Research Unit, Diabetes Center and Department of Medicine, University of California, San Francisco, California, 94143-0540 and the ^¶ Departments of Medicine and Cell Biology, National Science Foundation Center for Biological Timing, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908

Transcriptional regulation is commonly associated with local levels of histone acetylation, which controls chromatin structure at specific genes or within contiguous chromosomal domains. Less well understood are the higher order determinants of histone acetylation. The transcription factor, CCAAT/enhancer-binding protein  (C/EBP), concentrates at one higher order structure, the peri-centromeric chromatin, and regulates differentiation in many cell types, including pituitary cells. We used quantitative fluorescence microscopy to show that immunostained acetylated histone H3 is relatively absent from peri-centromeric domains visible as large structures in mouse pituitary progenitor GHFT1-5 cells. GHFT1-5 cells do not contain C/EBP. We observed that expression of C/EBP in GHFT1-5 cells leads to an increased level of acetylated histone H3, but not acetylated histone H4, at the peri-centromeric domains. Only transcriptionally active forms of C/EBP altered histone acetylation at the peri-centromeric domain. The altered state of histone acetylation at large intranuclear domains may complement, counteract, or supercede the more gene-local activities of other transcription factors to coordinate C/EBP-induced cellular differentiation.

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