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Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation

Author

Listed:
  • Harihar Basnet

    (Howard Hughes Medical Institute, University of California San Diego
    Biomedical Sciences Graduate Program, School of Medicine, University of California San Diego)

  • Xue B. Su

    (Section of Molecular Biology, UCSD Moores Cancer Center, University of California San Diego)

  • Yuliang Tan

    (Howard Hughes Medical Institute, University of California San Diego)

  • Jill Meisenhelder

    (Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies)

  • Daria Merkurjev

    (Howard Hughes Medical Institute, University of California San Diego
    Bioinformatics and Systems Biology Program, University of California San Diego)

  • Kenneth A. Ohgi

    (Howard Hughes Medical Institute, University of California San Diego)

  • Tony Hunter

    (Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies)

  • Lorraine Pillus

    (Section of Molecular Biology, UCSD Moores Cancer Center, University of California San Diego)

  • Michael G. Rosenfeld

    (Howard Hughes Medical Institute, University of California San Diego)

Abstract

A conserved tyrosine residue, Tyr 57, of histone H2A is phosphorylated by an unsuspected tyrosine kinase activity of casein kinase 2, influencing a series of histone marks associated with active transcription and regulating transcription elongation.

Suggested Citation

  • Harihar Basnet & Xue B. Su & Yuliang Tan & Jill Meisenhelder & Daria Merkurjev & Kenneth A. Ohgi & Tony Hunter & Lorraine Pillus & Michael G. Rosenfeld, 2014. "Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation," Nature, Nature, vol. 516(7530), pages 267-271, December.
    • Handle: RePEc:nat:nature:v:516:y:2014:i:7530:d:10.1038_nature13736
    DOI: 10.1038/nature13736
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