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

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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. and Rito, T. and Torlai Triglia, E. and Kukalev, A. and Ferrai, C. and Chotalia, M. and Brookes, E. and 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 (U.K.)
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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