作者
Joao D Dias, Tiago Rito, Elena Torlai Triglia, Alexander Kukalev, Carmelo Ferrai, Mita Chotalia, Emily Brookes, Hiroshi Kimura, Ana Pombo
发表日期
2015/12/19
期刊
Elife
卷号
4
页码范围
e11215
出版商
eLife Sciences Publications, Ltd
简介
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.
DOI: http://dx.doi.org/10.7554/eLife.11215.001
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JD Dias, T Rito, E Torlai Triglia, A Kukalev, C Ferrai… - Elife, 2015