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Journal Article

Heptad-specific phosphorylation of RNA polymerase II CTD.

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2245696.pdf
(Publisher version), 2MB

Supplementary Material (public)

2245696_Suppl_1.pdf
(Supplementary material), 2MB

2245696_Suppl_2.pdf
(Supplementary material), 4MB

Citation

Schüller, R., Forné, I., Straub, T., Schreieck, A., Texier, Y., Shah, N., et al. (2016). Heptad-specific phosphorylation of RNA polymerase II CTD. Molecular Cell, 61(2), 305-314. doi:10.1016/j.molcel.2015.12.003.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-69F1-6
Abstract
The carboxy-terminal domain (CTD) of RNA polymerase II (Pol II) consists of heptad repeats with the consensus motif Y1-S2-P3-T4-S5-P6-S7. Dynamic phosphorylation of the CTD coordinates Pol II progression through the transcription cycle. Here, we use genetic and mass spectrometric approaches to directly detect and map phosphosites along the entire CTD. We confirm phosphorylation of CTD residues Y1, S2, T4, S5, and S7 in mammalian and yeast cells. Although specific phosphorylation signatures dominate, adjacent CTD repeats can be differently phosphorylated, leading to a high variation of coexisting phosphosites in mono- and di-heptad CTD repeats. Inhibition of CDK9 kinase specifically reduces S2 phosphorylation levels within the CTD.