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First published online October 27, 2005
doi: 10.1242/10.1242/jcs.02621
Research Article |
í Pacherník2
arová1
Kovaík1íková1
1 Institute of Biophysics, Academy of Sciences of the Czech Republic, Královopolská 135, 612 65, Brno, Czech Republic
2 Center for Cell Therapy and Tissue Repair, Charles University, Vúvalu 84, 150 06 Prague 5, Czech Republic, and Laboratory of Molecular Embryology, Mendel University Brno, Zem
dlská 1, 613 00 Brno, Czech Republic
3 Faculty of Informatics, Masaryk University Brno, Botanická 68a, Czech Republic
* Author for correspondence (e-mail: kozubek{at}ibp.cz)
Accepted 3 August 2005
The effects of the histone deacetylase inhibitors (HDACi) trichostatin A (TSA) and sodium butyrate (NaBt) were studied in A549, HT29 and FHC human cell lines. Global histone hyperacetylation, leading to decondensation of interphase chromatin, was characterized by an increase in H3(K9) and H3(K4) dimethylation and H3(K9) acetylation. The levels of all isoforms of heterochromatin protein, HP1, were reduced after HDAC inhibition. The observed changes in the protein levels were accompanied by changes in their interphase patterns. In control cells, H3(K9) acetylation and H3(K4) dimethylation were substantially reduced to a thin layer at the nuclear periphery, whereas TSA and NaBt caused the peripheral regions to become intensely acetylated at H3(K9) and dimethylated at H3(K4). The dispersed pattern of H3(K9) dimethylation was stable even at the nuclear periphery of HDACi-treated cells. After TSA and NaBt treatment, the HP1 proteins were repositioned more internally in the nucleus, being closely associated with interchromatin compartments, while centromeric heterochromatin was relocated closer to the nuclear periphery. These findings strongly suggest dissociation of HP1 proteins from peripherally located centromeres in a hyperacetylated and H3(K4) dimethylated environment. We conclude that inhibition of histone deacetylases caused dynamic reorganization of chromatin in parallel with changes in its epigenetic modifications.
Key words: Histone dimethylation, Histone acetylation, HP1 proteins, HDAC inhibitors, Nuclear periphery
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