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@article{599184,
author = {Bártová, Eva and Pacherník, J. and Harničarová, Andrea and Kovařík, A. and Kovaříková, M. and Hofmanová, Jiřina and Skalníková, Magdalena and Kozubek, Michal and Kozubek, Stanislav},
article_location = {Cambridge},
article_number = {21},
keywords = {histone dimethylation; histone acetylation; HP1 proteins; HDAC inhibitors; nuclear periphery},
language = {eng},
issn = {0021-9533},
journal = {Journal of Cell Science},
title = {Nuclear levels and patterns of histone H3 modification and HP1 proteins after inhibition of histone deacetylases},
volume = {118},
year = {2005}
}
TY - JOUR
ID - 599184
AU - Bártová, Eva - Pacherník, J. - Harničarová, Andrea - Kovařík, A. - Kovaříková, M. - Hofmanová, Jiřina - Skalníková, Magdalena - Kozubek, Michal - Kozubek, Stanislav
PY - 2005
TI - Nuclear levels and patterns of histone H3 modification and HP1 proteins after inhibition of histone deacetylases
JF - Journal of Cell Science
VL - 118
IS - 21
SP - 5035-5046
EP - 5035-5046
PB - Company of Biologists Ltd.
SN - 00219533
KW - histone dimethylation
KW - histone acetylation
KW - HP1 proteins
KW - HDAC inhibitors
KW - nuclear periphery
N2 - 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.
ER -
BÁRTOVÁ, Eva, J. PACHERNÍK, Andrea HARNIČAROVÁ, A. KOVAŘÍK, M. KOVAŘÍKOVÁ, Jiřina HOFMANOVÁ, Magdalena SKALNÍKOVÁ, Michal KOZUBEK and Stanislav KOZUBEK. Nuclear levels and patterns of histone H3 modification and HP1 proteins after inhibition of histone deacetylases. \textit{Journal of Cell Science}. Cambridge: Company of Biologists Ltd., 2005, vol.~118, No~21, p.~5035-5046. ISSN~0021-9533.
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