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Nat Rev Mol Cell Biol. 2017 Mar;18(3):141-158. doi: 10.1038/nrm.2016.159. Epub 2017 Jan 5.

Histone chaperone networks shaping chromatin function.

Author information

1
Biotech Research and Innovation Centre (BRIC) and Centre for Epigenetics, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen DK-2200, Denmark.
2
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA.

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.

PMID:
28053344
PMCID:
PMC5319910
DOI:
10.1038/nrm.2016.159
[Indexed for MEDLINE]
Free PMC Article

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