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Brd4 activates P-TEFb for RNA polymerase II CTD phosphorylation.

Nucleic Acids Res

July 2014

Max Planck Institute of Molecular Physiology, Department of Physical Biochemistry, 44227 Dortmund, Germany Center of Advanced European Studies and Research (caesar), Group Physical Biochemistry, 53175 Bonn, Germany

The bromodomain protein Brd4 regulates the transcription of signal-inducible genes. This is achieved by recruiting the positive transcription elongation factor P-TEFb to promoters by its P-TEFb interaction domain (PID). Here we show that Brd4 stimulates the kinase activity of P-TEFb for phosphorylation of the C-terminal domain (CTD) of RNA polymerase II over basal levels.

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