Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation

被引：0
|
作者：
Harihar Basnet
Xue B. Su
Yuliang Tan
Jill Meisenhelder
Daria Merkurjev
Kenneth A. Ohgi
Tony Hunter
Lorraine Pillus
Michael G. Rosenfeld
机构：
[1] Howard Hughes Medical Institute,Department of Medicine
[2] University of California San Diego,Division of Biological Sciences
[3] Biomedical Sciences Graduate Program,Department of Bioengineering
[4] School of Medicine,undefined
[5] University of California San Diego,undefined
[6] Section of Molecular Biology,undefined
[7] UCSD Moores Cancer Center,undefined
[8] University of California San Diego,undefined
[9] Bioinformatics and Systems Biology Program,undefined
[10] University of California San Diego,undefined
[11] Molecular and Cell Biology Laboratory,undefined
[12] Salk Institute for Biological Studies,undefined
来源：
Nature | 2014年 / 516卷
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学科分类号：
摘要：
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.
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页码：267 / 271
页数：4
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