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10.1038/nrm.2016.159

http://scihub22266oqcxt.onion/10.1038/nrm.2016.159
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C5319910!5319910!28053344
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suck abstract from ncbi


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pmid28053344      Nat+Rev+Mol+Cell+Biol 2017 ; 18 (3): 141-58
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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): 141-58 PMID28053344show 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.
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