Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation

Harihar Basnet, Xue B. Su, Yuliang Tan, Jill Meisenhelder, Daria Merkurjev, Kenneth A. Ohgi, Tony Hunter, Lorraine Pillus () and Michael G. Rosenfeld ()
Additional contact information
Harihar Basnet: Howard Hughes Medical Institute, 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
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

Nature, 2014, vol. 516, issue 7530, 267-271

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.

Date: 2014
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DOI: 10.1038/nature13736

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