Histone chaperone networks shaping chromatin function Journal Article


Authors: Hammond, C. M.; Strømme, C. B.; Huang, H.; Patel, D. J.; Groth, A.
Article Title: Histone chaperone networks shaping chromatin function
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.
Keywords: transcription elongation; replication fork; saccharomyces-cerevisiae; rna-polymerase-ii; structural basis; dna-damage response; cenp-a; nucleosome assembly pathway; helicase subunit mcm2; tousled-like kinases
Journal Title: Nature Reviews Molecular Cell Biology
Volume: 18
Issue: 3
ISSN: 1471-0072
Publisher: Nature Publishing Group  
Date Published: 2017-03-01
Start Page: 141
End Page: 158
Language: English
ACCESSION: WOS:000394569200007
DOI: 10.1038/nrm.2016.159
PROVIDER: wos
PMCID: PMC5319910
PUBMED: 28053344
Notes: Review -- Source: Wos
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  1. Dinshaw J Patel
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  2. Hongda Huang
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