Histone chaperone networks shaping chromatin function

Publikation: Bidrag til tidsskriftReviewForskningfagfællebedømt

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

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.

TidsskriftNature Reviews. Molecular Cell Biology
Udgave nummer3
Sider (fra-til)141-158
Antal sider18
StatusUdgivet - mar. 2017

ID: 174434845