Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly

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 phosphorylati...

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Published inGenes & development Vol. 25; no. 13; pp. 1359 - 1364
Main Authors Kang, Bin, Pu, Mintie, Hu, Gangqing, Wen, Weihong, Dong, Zigang, Zhao, Keji, Stillman, Bruce, Zhang, Zhiguo
Format Journal Article
LanguageEnglish
Published United States Cold Spring Harbor Laboratory Press 01.07.2011
Subjects
Amino acids
Cell Cycle Proteins - metabolism
Chromatin - metabolism
HEK293 Cells
HeLa Cells
Histone Chaperones - metabolism
Histones - metabolism
Humans
Nucleosomes - metabolism
p21-Activated Kinases
Phosphorylation
Protein Binding
Research Communication
Serine - metabolism
Transcription Factors - metabolism
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Summary: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.
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These authors contributed equally to this work.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.2055511