The DNA intercalators ethidium bromide and propidium iodide also bind to core histones

•DNA intercalators ethidium bromide and propidium iodide also bind to core histones.•These ligands release DNA from the chromatosome.•These ligands cause chromatin compaction.•These ligands alter the acetylation status of histones H3 and H4. Eukaryotic DNA is compacted in the form of chromatin, in a...

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Bibliographic Details
Published in:FEBS open bio 2014-01, Vol.4 (1), p.251-259
Main Authors: Banerjee, Amrita, Majumder, Parijat, Sanyal, Sulagna, Singh, Jasdeep, Jana, Kuladip, Das, Chandrima, Dasgupta, Dipak
Format: Article
Language:English
Subjects:
Acetylation
Binding sites
Chromatin
Chromatin compaction
Deoxyribonucleic acid
DNA
DNA methylation
DNA release
Ethidium bromide
Histone acetylation
Histone and DNA binding
Histone H3
Histone H4
Ligands
Lysine
Propidium iodide
Proteins
Spectrum analysis
Structure-function relationships
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Summary:•DNA intercalators ethidium bromide and propidium iodide also bind to core histones.•These ligands release DNA from the chromatosome.•These ligands cause chromatin compaction.•These ligands alter the acetylation status of histones H3 and H4. Eukaryotic DNA is compacted in the form of chromatin, in a complex with histones and other non-histone proteins. The intimate association of DNA and histones in chromatin raises the possibility that DNA-interactive small molecules may bind to chromatin-associated proteins such as histones. Employing biophysical and biochemical techniques we have characterized the interaction of a classical intercalator, ethidium bromide (EB) and its structural analogue propidium iodide (PI) with hierarchical genomic components: long chromatin, chromatosome, core octamer and chromosomal DNA. Our studies show that EB and PI affect both chromatin structure and function, inducing chromatin compaction and disruption of the integrity of the chromatosome. Calorimetric studies and fluorescence measurements of the ligands demonstrated and characterized the association of these ligands with core histones and the intact octamer in absence of DNA. The ligands affect acetylation of histone H3 at lysine 9 and acetylation of histone H4 at lysine 5 and lysine 8 ex vivo. PI alters the post-translational modifications to a greater extent than EB. This is the first report showing the dual binding (chromosomal DNA and core histones) property of a classical intercalator, EB, and its longer analogue, PI, in the context of chromatin.
ISSN:2211-5463
2211-5463
DOI:10.1016/j.fob.2014.02.006