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Journal Article

RNA polymerase II clustering through carboxy-terminal domain phase separation.

MPS-Authors
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Boehning,  M.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons186186

Kokic,  G.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons127020

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

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Supplementary Material (public)

2637708_Suppl_1.pdf
(Supplementary material), 2MB

2637708_Suppl_2.pdf
(Supplementary material), 124KB

2637708_Suppl_3.pdf
(Supplementary material), 3MB

2637708_Suppl_4.pdf
(Supplementary material), 12MB

2637708_Suppl_5.mpg
(Supplementary material), 476KB

2637708_Suppl_6.mpg
(Supplementary material), 238KB

2637708_Suppl_7.avi
(Supplementary material), 7MB

2637708_Suppl_8.avi
(Supplementary material), 7MB

2637708_Suppl_9.avi
(Supplementary material), 6MB

2637708_Suppl_10.mpg
(Supplementary material), 2MB

Citation

Boehning, M., Dugast-Darzacq, C., Rankovic, M., Hansen, A. S., Yu, T., Marie-Nelly, H., et al. (2018). RNA polymerase II clustering through carboxy-terminal domain phase separation. Nature Structural and Molecular Biology, 25, 833-840. doi:10.1038/s41594-018-0112-y.


Cite as: https://hdl.handle.net/21.11116/0000-0001-FF7D-5
Abstract
The carboxy-terminal domain (CTD) of RNA polymerase (Pol) II is an intrinsically disordered low-complexity region that is critical for pre-mRNA transcription and processing. The CTD consists of hepta-amino acid repeats varying in number from 52 in humans to 26 in yeast. Here we report that human and yeast CTDs undergo cooperative liquid phase separation, with the shorter yeast CTD forming less-stable droplets. In human cells, truncation of the CTD to the length of the yeast CTD decreases Pol II clustering and chromatin association, whereas CTD extension has the opposite effect. CTD droplets can incorporate intact Pol II and are dissolved by CTD phosphorylation with the transcription initiation factor IIH kinase CDK7. Together with published data, our results suggest that Pol II forms clusters or hubs at active genes through interactions between CTDs and with activators and that CTD phosphorylation liberates Pol II enzymes from hubs for promoter escape and transcription elongation.