The histone-DNA interaction is found to greatly improve the fluorescence intensity and stability of DNA-templated Cu nanoclusters (CuNCs), which would be highly beneficial for the application of CuNCs in biosensing/imaging.
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Ion pairing in aqueous tetramethylammonium-acetate solutions by neutron scattering and molecular dynamics simulations.
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Université Paris Cité, CNRS, Laboratoire de Biochimie Théorique, 13 rue Pierre et Marie Curie, 75005, Paris, France.
Tetramethylammonium (TMA) is a ubiquitous cationic motif in biochemistry, found in the charged choline headgroup of membrane phospholipids and in tri-methylated lysine residues, which modulates histone-DNA interactions and impacts epigenetic mechanisms. TMA interactions with anionic species, particularly carboxylate groups of amino acid residues and extracellular sugars, are of substantial biological relevance, as these interactions mediate a wide range of cellular processes. This study investigates the molecular interactions between TMA and acetate, representing carboxylate-containing groups, using neutron scattering experiments complemented by force fields and molecular dynamics (MD) simulations.
View Article and Find Full Text PDFA versatile approach for geometry-based self-assembly of DNA-protein hybrid nanostructures using histone-DNA interactions.
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January 2025
King Abdullah University of Science and Technology, Biological and Environmental Science and Engineering Division, Thuwal 23955-6900, Saudi Arabia.
We report an enhanced versatility in constructing DNA-protein hybrid nanostructures using histone-DNA complexes (HDs). By leveraging HDs, we demonstrate precise and scalable assembly of DNA origami tiles and a 2D triangular nanostructure. Our results extend the potential applications of DNA nanotechnology from the nanoscale to the microscale without the need for complex pre-designs.
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N.N. Blokhin National Medical Research Center of Oncology, Ministry of Health of Russia, 115478 Moscow, Russia.
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Methods: Nucleosome stability and linker histone H1.
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Department of Epigenetics, Van Andel Research Institute, Grand Rapids, MI 49503, USA.
The incorporation of histone variants has structural ramifications on nucleosome dynamics and stability. Due to their unique sequences, histone variants can alter histone-histone or histone-DNA interactions, impacting the folding of DNA around the histone octamer and the overall higher-order structure of chromatin fibers. These structural modifications alter chromatin compaction and accessibility of DNA by transcription factors and other regulatory proteins to influence gene regulatory processes such as DNA damage and repair, as well as transcriptional activation or repression.
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Article Synopsis
- - Each nucleosome is made up of four types of histone proteins, and their tails are vital for regulating gene expression through modifications after protein synthesis (PTMs).
- - Using high-speed atomic force microscopy, researchers studied nucleosome dynamics when histone tails were removed, finding that the absence of all tails caused significant structural changes and increased flexibility in nucleosome behavior.
- - The study revealed that histone tails, especially from H2B and H3, stabilize nucleosomes and their post-translational modifications play a key role in how nucleosomes interact with DNA.
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