Department of Biochemistry & Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Cell Rep. 2018 Dec 18;25(12):3476-3489.e5. doi: 10.1016/j.celrep.2018.11.089.
Spt6 is a histone chaperone that associates with RNA polymerase II and deposits nucleosomes in the wake of transcription. Although Spt6 has an essential function in nucleosome deposition, it is not known whether this function is influenced by post-translational modification. Here, we report that casein kinase II (CKII) phosphorylation of Spt6 is required for nucleosome occupancy at the 5' ends of genes to prevent aberrant antisense transcription and enforce transcriptional directionality. Mechanistically, we show that CKII phosphorylation of Spt6 promotes the interaction of Spt6 with Spn1, a binding partner required for chromatin reassembly and full recruitment of Spt6 to genes. Our study defines a function for CKII phosphorylation in transcription and highlights the importance of post-translational modification in histone chaperone function.
Spt6 是一种组蛋白伴侣，它与 RNA 聚合酶 II 结合，并在转录后在核小体中沉积。尽管 Spt6 在核小体沉积中具有重要功能，但尚不清楚这种功能是否受到翻译后修饰的影响。在这里，我们报告说，酪蛋白激酶 II（CKII）对 Spt6 的磷酸化是防止异常反义转录和强制转录方向性所必需的，以确保基因 5' 端的核小体占有率。从机制上讲，我们表明，Spt6 的 CKII 磷酸化促进了 Spt6 与 Spn1 的相互作用，Spn1 是染色质重排和 Spt6 完全招募到基因所必需的结合伴侣。我们的研究定义了 CKII 磷酸化在转录中的功能，并强调了翻译后修饰在组蛋白伴侣功能中的重要性。
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