Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7.

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.
Science (Impact Factor: 31.48). 01/2008; 318(5857):1780-2. DOI: 10.1126/science.1145977
Source: PubMed

ABSTRACT 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.

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Available from: Thomas K Albert, Jun 28, 2015
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