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Science 14 December 2007:
Vol. 318. no. 5857, pp. 1780 - 1782
DOI: 10.1126/science.1145977
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Reports

Transcribing RNA Polymerase II Is Phosphorylated at CTD Residue Serine-7

Rob D. Chapman,1 Martin Heidemann,1 Thomas K. Albert,2* Reinhard Mailhammer,1 Andrew Flatley,2 Michael Meisterernst,2* Elisabeth Kremmer,2 Dirk Eick1{dagger}

RNA polymerase II is distinguished by its large carboxyl-terminal repeat domain (CTD), composed of repeats of the consensus heptapeptide Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. Differential phosphorylation of serine-2 and serine-5 at the 5' and 3' regions of genes appears to coordinate the localization of transcription and RNA processing factors to the elongating polymerase complex. Using monoclonal antibodies, we reveal serine-7 phosphorylation on transcribed genes. This position does not appear to be phosphorylated in CTDs of less than 20 consensus repeats. The position of repeats where serine-7 is substituted influenced the appearance of distinct phosphorylated forms, suggesting functional differences between CTD regions. Our results indicate that restriction of serine-7 epitopes to the Linker-proximal region limits CTD phosphorylation patterns and is a requirement for optimal gene expression.

1 Institute of Clinical Molecular Biology and Tumour Genetics, GSF-Research Center of Environment and Health, Munich Center for Integrated Protein Science (CiPSM), Marchioninistrasse 25, 81377 Munich, Germany.
2 Institute of Molecular Immunology, GSF-Research Center of Environment and Health, Munich Center for Integrated Protein Science, Marchioninistrasse 25, 81377 Munich, Germany.

* Present address: Institute of Tumor Biology, University Muenster, Robert-Koch-Strasse 43, 48149 Muenster, Germany.

{dagger} To whom correspondence should be addressed. E-mail: eick{at}gsf.de

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Serine-7 of the RNA Polymerase II CTD Is Specifically Required for snRNA Gene Expression.
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Science 318, 1777-1779
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