ArticleFEBS open bio2014
The DNA intercalators ethidium bromide and propidium iodide also bind to core histones.
Article in FEBS open bio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 87 citations in OpenAlex.
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- Application of the SwitchSense Technique for the Study of Small Molecules' (Ethidium Bromide and Selected Sulfonamide Derivatives) Affinity to DNA in Real Time.The journal of physical chemistry. B · 2022Article
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- Corrigendum to: The DNA intercalators ethidium bromide and propidium iodide also bind to core histones.FEBS open bio · 2022Article
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- Class I defensins (BraDef) from broccoli (Brassica oleracea var. italica) seeds and their antimicrobial activity.World journal of microbiology & biotechnology · 2020Article
- Article
- A Comprehensive Biophysical Analysis of the Effect of DNA Binding Drugs on Protamine-induced DNA Condensation.Scientific reports · 2019Article
- Intercalation of small molecules into DNA in chromatin is primarily controlled by superhelical constraint.PloS one · 2019Article
- L-Asparaginase of Leishmania donovani: Metabolic target and its role in Amphotericin B resistance.International journal for parasitology. Drugs and drug resistance · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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