Histone chaperone networks shaping chromatin function

Colin Hammond, Caroline Bianchi Strømme, Hongda Huang, Dinshaw J Patel, Anja Groth

    185 Citationer (Scopus)

    Abstract

    The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin.

    OriginalsprogEngelsk
    TidsskriftNature Reviews. Molecular Cell Biology
    Vol/bind18
    Udgave nummer3
    Sider (fra-til)141-158
    Antal sider18
    ISSN1471-0072
    DOI
    StatusUdgivet - 1 mar. 2017

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