Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction

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

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Dronamraju et al. show that the N terminus of Spt6 is phosphorylated by casein kinase II, which is required for proper Spt6-Spn1 interaction. CKII phosphorylation of Spt6 is pivotal to maintain nucleosome occupancy at the 5′ ends of genes, suppression of antisense transcription from the 5′ ends, and resistance to genotoxic agents.

Original languageEnglish (US)
Pages (from-to)3476-3489.e5
JournalCell Reports
Volume25
Issue number12
DOIs
StatePublished - Dec 18 2018

Keywords

  • CKII
  • SILAC
  • Spn1
  • Spt6
  • nucleosome occupancy

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Dronamraju, R., Kerschner, J. L., Peck, S. A., Hepperla, A. J., Adams, A. T., Hughes, K. D., Aslam, S., Yoblinski, A. R., Davis, I. J., Mosley, A. L., & Strahl, B. D. (2018). Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction. Cell Reports, 25(12), 3476-3489.e5. https://doi.org/10.1016/j.celrep.2018.11.089