Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly

Bin Kang, Mintie Pu, Gangqing Hu, Weihong Wen, Zigang Dong, Keji Zhao, Bruce Stillman, Zhiguo Zhang

Research output: Contribution to journalArticle

42 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1359-1364
Number of pages6
JournalGenes and Development
Volume25
Issue number13
DOIs
StatePublished - Jul 1 2011

Keywords

  • CAF-1
  • HIRA
  • Histone H3.3
  • Histone variant
  • Nucleosome assembly
  • PAK2

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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    Kang, B., Pu, M., Hu, G., Wen, W., Dong, Z., Zhao, K., Stillman, B., & Zhang, Z. (2011). Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly. Genes and Development, 25(13), 1359-1364. https://doi.org/10.1101/gad.2055511