| Literature DB >> 21724829 |
Bin Kang1, Mintie Pu, Gangqing Hu, Weihong Wen, Zigang Dong, Keji Zhao, Bruce Stillman, Zhiguo Zhang.
Abstract
Histone H3 variant H3.3, while differing from canonical H3 (H3.1) by only five amino acids, is assembled into nucleosomes, along with histone H4, at genic regions by the histone chaperone HIRA, whereas H3.1 is assembled into nucleosomes in a CAF-1-dependent reaction. Here, we show that phosphorylation of histone H4 Ser 47 (H4S47ph), catalyzed by the PAK2 kinase, promotes nucleosome assembly of H3.3-H4 and inhibits nucleosome assembly of H3.1-H4 by increasing the binding affinity of HIRA to H3.3-H4 and reducing association of CAF-1 with H3.1-H4. These results reveal a mechanism whereby H4S47ph distinctly regulates nucleosome assembly of H3.1 and H3.3.Entities:
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Year: 2011 PMID: 21724829 PMCID: PMC3134079 DOI: 10.1101/gad.2055511
Source DB: PubMed Journal: Genes Dev ISSN: 0890-9369 Impact factor: 11.361