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Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability

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Author(s)

Helder Ferreira, Joanna Somers, Ryan Webster, Andrew Flaus, Tom Owen-Hughes

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Abstract

Nucleosomes fulfill the apparently conflicting roles of compacting DNA within eukaryotic genomes while permitting access to regulatory factors. Central to this is their ability to stably associate with DNA while retaining the ability to undergo rearrangements that increase access to the underlying DNA. Here, we have studied different aspects of nucleosome dynamics including nucleosome sliding, histone dimer exchange, and DNA wrapping within nucleosomes. We find that alterations to histone proteins, especially the histone tails and vicinity of the histone H3 alpha N helix, can affect these processes differently, suggesting that they are mechanistically distinct. This raises the possibility that modifications to histone proteins may provide a means of fine-tuning specific aspects of the dynamic properties of nucleosomes to the context in which they are located.

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Original languageEnglish
Pages (from-to)4037-4048
Number of pages12
JournalMolecular and Cellular Biology
Volume27
Issue number11
DOIs
Publication statusPublished - Jun 2007

    Research areas

  • BASE-PAIR RESOLUTION, SACCHAROMYCES-CEREVISIAE, CORE PARTICLE, LINKER DNA, POSTTRANSLATIONAL MODIFICATIONS, LYSINE-56 ACETYLATION, ANGSTROM RESOLUTION, TERMINAL TAILS, CHROMATIN, TRANSCRIPTION

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