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2017 ; 18
(3
): 141-158
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Histone chaperone networks shaping chromatin function
#MMPMID28053344
Hammond CM
; Strømme CB
; Huang H
; Patel DJ
; Groth A
Nat Rev Mol Cell Biol
2017[Mar]; 18
(3
): 141-158
PMID28053344
show ga
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.