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  Heptad-specific phosphorylation of RNA polymerase II CTD.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-69F1-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-1B9C-1
Genre: Journal Article

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 Creators:
Schüller, R., Author
Forné, I., Author
Straub, T., Author
Schreieck, A., Author
Texier, Y., Author
Shah, N., Author
Decker, T. M., Author
Cramer, P.1, Author              
Imhof, A., Author
Eick, D., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 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.

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Language(s): eng - English
 Dates: 2016-01-212016-01-21
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2015.12.003
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 61 (2) Sequence Number: - Start / End Page: 305 - 314 Identifier: -