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- W2912268225 abstract "Oxidative damage to DNA by reactive oxygen species (ROS) can result in the formation of the highly mutagenic Spiroiminodihydantoin (Sp) lesion. The Sp lesion disrupts the shape of the DNA double helix due to the introduction of a propeller-like chiral center. If left unrepaired, oxidative stress is harmful to DNA stability as it may lead to permanent mutations, cancer, cellular aging or apoptosis. Our lab has previously demonstrated that Sp lesions cause subtle changes in nucleosome stability and positioning. Nucleosomes are formed when ∼146 base pairs of DNA are wrapped around octamers of histone proteins. These structures compact our DNA and control access by repair proteins, transcription factors, and polymerases. We are using Fluroescence Resonance Energy Transfer (FRET) to explore in more detail how the Sp lesion influences nucleosome assembly and disassembly. We synthesized and characterized 146-mer duplexes with Cy3 and Cy5 fluorphores and Sp lesions at various locations, allowing us to assemble a variety of nucleosome core particles containing fluorescent donor-acceptor pairs. In undamaged nucleosomes, FRET occurs between the donor and acceptor fluorophores consistent with their proximity; gradual unfolding of the nucleosomes by titration with NaCl leads to a loss in acceptor fluorescence, consistent with peeling of the DNA ends from the histone octamer surface. We are measuring quantitatively the correlation between the stability of the nucleosome and presence and location of the lesion and hope to elucidate whether the histone tetramer or dimer is more sensitive to DNA distortions. These experiments will advance our understanding of how the Sp lesion affects the process of DNA compaction into nucleosomes." @default.
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- W2912268225 date "2019-02-01" @default.
- W2912268225 modified "2023-10-16" @default.
- W2912268225 title "Studying Nucleosome Assembly via FRET" @default.
- W2912268225 doi "https://doi.org/10.1016/j.bpj.2018.11.1176" @default.
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