Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome

Ramasubramanian Sundaramoorthy, Amanda Hughes, Hassane El-Mkami, David Norman, Thomas Owen-Hughes (Lead / Corresponding author)

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    52 Citations (Scopus)
    223 Downloads (Pure)

    Abstract

    ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein-DNA interactions. Here we present structures of the Saccharomyces cerevisiae Chd1 protein engaged with nucleosomes in the presence of the transition state mimic ADP-beryllium fluoride. The path of DNA strands through the ATPase domains indicates the presence of contacts conserved with single strand translocases and additional contacts with both strands that are unique to Snf2 related proteins. The structure provides connectivity between rearrangement of ATPase lobes to a closed, nucleotide bound state and the sensing of linker DNA. Two turns of linker DNA are prised off the surface of the histone octamer as a result of Chd1 binding, and both the histone H3 tail and ubiquitin conjugated to lysine 120 are re-orientated towards the unravelled DNA. This indicates how changes to nucleosome structure can alter the way in which histone epitopes are presented.
    Original languageEnglish
    Article numbere35720
    Pages (from-to)1-28
    Number of pages28
    JournaleLife
    Volume2018
    Issue number7
    Early online date6 Aug 2018
    DOIs
    Publication statusPublished - 6 Aug 2018

    ASJC Scopus subject areas

    • General Neuroscience
    • General Biochemistry,Genetics and Molecular Biology
    • General Immunology and Microbiology

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