Histone chaperone networks shaping chromatin function

• Published in: Nature reviews. Molecular cell biology Vol. 18; no. 3; pp. 141 - 158
• Main Authors: Hammond, Colin M., Strømme, Caroline B., Huang, Hongda, Patel, Dinshaw J., Groth, Anja
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.03.2017; Nature Publishing Group
• Subjects: 631/337/100/1701; 631/337/100/2286; 631/337/151; 631/337/470/1981; Animals; Biochemistry; Biology; Cancer Research; Cell Biology; Cell cycle; Chromatin; Chromatin - physiology; Developmental Biology; DNA Replication; Epigenetics; Genomes; Histone Chaperones - chemistry; Histone Chaperones - genetics; Histone Chaperones - metabolism; Histones; Histones - genetics; Histones - metabolism; Humans; Life Sciences; Molecular chaperones; Nucleosomes - chemistry; Nucleosomes - metabolism; Proteins; review-article; Stem Cells; Yeast; New York; United States > US
• ISSN: 1471-0072; 1471-0080
• DOI: 10.1038/nrm.2016.159

Key Points Chromatin integrity and functionality is governed by the controlled assembly and disassembly of nucleosomes. An elaborate histone chaperone network governs histone provision, chromatin assembly, histone recycling and histone turnover. Histone chaperone networks operate through histone-dependent co-chaperone interactions and direct chaperone–chaperone contacts. The mode of action of histone chaperones is interpreted from structural and biochemical studies of histone–chaperone complexes. Key molecular functions of histone chaperones include the shielding of functional histone interfaces and trapping histones in non-nucleosomal conformations. The integration of histone chaperone function across DNA metabolic processes acts to maintain genome and epigenome integrity. Histone chaperones safeguard the chromatin template and shield histones from promiscuous interactions to ensure their proper storage, transport, post-translational modification, nucleosome assembly and turnover. 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.