Molecular Biology Reports

, Volume 39, Issue 1, pp 303–308

DNA damage in the presence of chemical genotoxic agents induce acetylation of H3K56 and H4K16 but not H3K9 in mammalian cells


DOI: 10.1007/s11033-011-0739-9

Cite this article as:
Vempati, R.K. Mol Biol Rep (2012) 39: 303. doi:10.1007/s11033-011-0739-9


Histone covalent modifications play a significant role in the regulation of chromatin structure and function during DNA damage. Hyperacetylation of histones is a DNA damage dependent post translational modification in yeast and mammals. Although acetylation of histones during DNA damage is well established, specific lysine residues that are acetylated is being understood very recently in mammals. Here, in the present study, acetylation of three different lysine residues Histone3Lysine 9 (H3K9), Histone3Lysine 56 (H3K56) and Histone4Lysine 16 (H4K16) were probed with specific antibodies in mammalian cell lines treated with genotoxic agents that induce replication stress or S-phase dependent double strand breaks. Immunoblotting results have shown that DNA damage associated with replication arrest induce acetylation of H3K56 and H4K16 but not H3K9 in mammals. Immunofluorescence experiments further confirmed that acetylated H3K56 and H4K16 form nuclear foci at the site of DNA double strand breaks. Colocalization of H3K56ac with γ H2AX and replication factor PCNA proved the existence of this modification at the site of DNA damage and its probable role in DNA damage repair. Put together, the present data suggests that acetylation of H3K56 and H4K16 are potent DNA damage dependent histone modifications but not H3K9 in mammals.


DNA damage Histone modifications Acetylation 

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  1. 1.Epigenetics and Cancer Biology Lab, Institute of Life SciencesUniversity of HyderabadGachibowli, HyderabadIndia
  2. 2.Department of Medicine, Hematology and Oncology and Interdisciplinary Center for Clinical Research (IZKF)University of MünsterMünsterGermany

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