Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction
Year: 2018
Type: article
Abstract: 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.
Source: Cell Reports
Authors: Raghuvar Dronamraju, Jenny L. Kerschner, Sarah A. Peck, Austin J. Hepperla, Alexander T. Adams, Katlyn D. Hughes, Sadia Aslam, Andrew R. Yoblinski, Ian J. Davis, Amber L. Mosley, Brian D. Strahl
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,620
Awards: Regulation of RNA Polymerase II transcription by the phosphatase Rtr1, Chromatin maintenance in cancer progression, Quantitative Analysis of Transcription Elongation Perturbation Networks, Chromatin organization and transcription factor targeting in cancer, The Role of Spt6 in Genome Organization and Stability, Integrated Training in Cancer Model Systems, G4357829143, Mechanisms of chromatin and transcriptional regulation
OpenAlex ID: W2905374156