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Elife. 2015 Dec 19;4. pii: e11215. doi: 10.7554/eLife.11215.

Methylation of RNA polymerase II non-consensus Lysine residues marks early transcription in mammalian cells.

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Epigenetic Regulation and Chromatin Architecture Group, Berlin Institute for Medical Systems Biology, Max-Delbrück Centre for Molecular Medicine, Berlin, Germany.
Genome Function Group, MRC Clinical Sciences Centre, Imperial College London, London, United Kingdom.
Graduate Program in Areas of Basic and Applied Biology, University of Porto, Porto, Portugal.
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.


Dynamic post-translational modification of RNA polymerase II (RNAPII) coordinates the co-transcriptional recruitment of enzymatic complexes that regulate chromatin states and processing of nascent RNA. Extensive phosphorylation of serine residues at the largest RNAPII subunit occurs at its structurally-disordered C-terminal domain (CTD), which is composed of multiple heptapeptide repeats with consensus sequence Y1-S2-P3-T4-S5-P6-S7. Serine-5 and Serine-7 phosphorylation mark transcription initiation, whereas Serine-2 phosphorylation coincides with productive elongation. In vertebrates, the CTD has eight non-canonical substitutions of Serine-7 into Lysine-7, which can be acetylated (K7ac). Here, we describe mono- and di-methylation of CTD Lysine-7 residues (K7me1 and K7me2). K7me1 and K7me2 are observed during the earliest transcription stages and precede or accompany Serine-5 and Serine-7 phosphorylation. In contrast, K7ac is associated with RNAPII elongation, Serine-2 phosphorylation and mRNA expression. We identify an unexpected balance between RNAPII K7 methylation and acetylation at gene promoters, which fine-tunes gene expression levels.


C-terminal domain; RNA polymerase II; chromosomes; computational biology; genes; methylation; mouse; non-histone protein lysine methylation; post-transcriptional modification; systems biology; transcription cycle

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