Histone H3 Glutathionylation in Proliferating Mammalian Cells Destabilizes Nucleosomal Structure
Publication: Antioxidants & Redox Signaling
Volume 19, Issue Number 12
Abstract
Aims: Here we report that chromatin, the complex and dynamic eukaryotic DNA packaging structure, is able to sense cellular redox changes. Histone H3, the only nucleosomal protein that possesses cysteine(s), can be modified by glutathione (GSH). Results: Using Biotin labeled glutathione ethyl ester (BioGEE) treatment of nucleosomes in vitro, we show that GSH, the most abundant antioxidant in mammals, binds to histone H3. BioGEE treatment of NIH3T3 cells indicates that glutathionylation of H3 is maximal in fast proliferating cells, correlating well with enhanced levels of H3 glutathionylation in different tumor cell lines. Furthermore, glutathionylation of H3 in vivo decreases in livers from aged SAMP8 and C57BL/6J mice. We demonstrate biochemically and by mass spectrometry that histone variants H3.2/H3.3 are glutathionylated on their cysteine residue 110. Furthermore, circular dichroism, thermal denaturation of reconstituted nucleosomes, and molecular modeling indicate that glutathionylation of histone H3 produces structural changes affecting nucleosomal stability. Innovation: We characterize the implications of histone H3 glutathionylation in cell physiology and the modulation of core histone proteins structure affected by this modification. Conclusion: Histone H3 senses cellular redox changes through glutathionylation of Cys, which increases during cell proliferation and decreases during aging. Glutathionylation of histone H3 affects nucleosome stability structure leading to a more open chromatin structure. Antioxid. Redox Signal. 19, 1305–1320.
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Published In
Antioxidants & Redox Signaling
Volume 19 • Issue Number 12 • October 20, 2013
Pages: 1305 - 1320
PubMed: 23541030
Copyright
Copyright 2013, Mary Ann Liebert, Inc.
History
Published in print: October 20, 2013
Published online: 4 October 2013
Published ahead of print: 21 May 2013
Published ahead of production: 31 March 2013
Accepted: 31 March 2013
Revision received: 12 March 2013
Received: 19 October 2012
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