Histone chaperone networks shaping chromatin function

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

doi:10.1038/nrm.2016.159

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.

Originalsprog	Engelsk
Tidsskrift	Nature Reviews. Molecular Cell Biology
Vol/bind	18
Udgave nummer	3
Sider (fra-til)	141-158
Antal sider	18
ISSN	1471-0072
DOI	https://doi.org/10.1038/nrm.2016.159
Status	Udgivet - 1 mar. 2017

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10.1038/nrm.2016.159

http://europepmc.org/articles/pmc5319910?pdf=renderLicens: Andet

Citationsformater

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AU - Patel, Dinshaw J

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N2 - 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.

AB - 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.

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Histone chaperone networks shaping chromatin function

Abstract

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