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| Item Type: | Article |
|---|---|
| Title: | Methylation of RNA polymerase II non-consensus Lysine residues marks early transcription in mammalian cells |
| Creators Name: | Dias, J.D., Rito, T., Torlai Triglia, E., Kukalev, A., Ferrai, C., Chotalia, M., Brookes, E., Kimura, H. and Pombo, A. |
| Abstract: | 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. |
| Keywords: | Transcription Cycle, Post-Transcriptional Modification, RNA Polymerase II, C-32 Terminal Domain, Methylation, Non-Histone Protein Lysine Methylation, Animals, Mice |
| Source: | eLife |
| ISSN: | 2050-084X |
| Publisher: | eLife Sciences Publications |
| Volume: | 4 |
| Page Range: | e11215 |
| Date: | 19 December 2015 |
| Official Publication: | https://doi.org/10.7554/eLife.11215 |
| PubMed: | View item in PubMed |
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