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- W2336701517 abstract "Abstract H1 linker histones are highly abundant proteins that compact nucleosomes and chromatin to regulate DNA accessibility and transcription. However, the mechanisms that target H1 regulation to specific regions of eukaryotic genomes are unknown. Here we report fluorescence measurements of human H1 regulation of nucleosome dynamics and transcription factor (TF) binding within nucleosomes. H1 does not block TF binding, instead it suppresses nucleosome unwrapping to reduce DNA accessibility within H1-bound nucleosomes. We then investigated H1 regulation by H3K56 and H3K122 acetylation, two transcriptional activating histone post translational modifications (PTMs). Only H3K56 acetylation, which increases nucleosome unwrapping, abolishes H1.0 reduction of TF binding. These findings show that nucleosomes remain dynamic, while H1 is bound and H1 dissociation is not required for TF binding within the nucleosome. Furthermore, our H3K56 acetylation measurements suggest that a single-histone PTM can define regions of the genome that are not regulated by H1." @default.
- W2336701517 created "2016-06-24" @default.
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- W2336701517 date "2015-12-09" @default.
- W2336701517 modified "2023-09-27" @default.
- W2336701517 title "Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics" @default.
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- W2336701517 doi "https://doi.org/10.1038/ncomms10152" @default.
- W2336701517 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4682114" @default.
- W2336701517 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26648124" @default.
- W2336701517 hasPublicationYear "2015" @default.
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