Acetylation of core histones in response to HDAC inhibitors is diminished in mitotic HeLa cells

JS Patzlaff, Edith Terrenoire, Bryan Turner, WC Earnshaw, JR Paulson

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11 Citations (Scopus)


Histone acetylation is a key modification that regulates chromatin accessibility. Here we show that treatment with butyrate or other histone deacetylase (HDAC) inhibitors does not induce histone hyperacetylation in metaphase-arrested HeLa cells. When compared to similarly treated interphase cells, acetylation levels are significantly decreased in all four core histones and at all individual sites examined. However, the extent of the decrease varies, ranging from only slight reduction at H3K23 and H4K12 to no acetylation at H3K27 and barely detectable acetylation at H4K16. Our results show that the bulk effect is not due to increased or butyrate-insensitive HDAC activity, though these factors may play a role with some individual sites. We conclude that the lack of histone acetylation during mitosis is primarily due to changes in histone acetyltransferases (HATs) or changes in chromatin. The effects of protein phosphatase inhibitors on histone acetylation in cell lysates suggest that the reduced ability of histones to become acetylated in mitotic cells depends on protein phosphorylation. (C) 2010 Elsevier Inc. All rights reserved.
Original languageEnglish
Pages (from-to)2123-2135
Number of pages13
JournalExperimental Cell Research
Issue number13
Publication statusPublished - 1 Aug 2010


  • HDAC inhibitors
  • Mitosis
  • Butyrate
  • Histone acetylation
  • Metaphase chromosomes
  • Protein phosphatases


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