Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Genes Dev. 2011 Jul 1;25(13):1359-64. doi: 10.1101/gad.2055511.
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.
组蛋白 H3 变体 H3.3 与经典组蛋白 H3（H3.1）仅相差五个氨基酸，由组蛋白伴侣 HIRA 与组蛋白 H4 一起组装到基因区域的核小体中，而 H3.1 则通过 CAF-1 依赖性反应组装到核小体中。在这里，我们表明 PAK2 激酶催化的组蛋白 H4 Ser 47（H4S47ph）的磷酸化，通过增加 HIRA 与 H3.3-H4 的结合亲和力和减少 CAF-1 与 H3.1-H4 的关联，促进 H3.3-H4 的核小体组装，并抑制 H3.1-H4 的核小体组装。这些结果揭示了一种机制，通过该机制，H4S47ph 明显调节 H3.1 和 H3.3 的核小体组装。
