Expanding the CTD code: methylation of non-consensus Lysine residues marks early transcription in mammalian cells

ABSTRACT: Dynamic post-translational modification of RNA polymerase II (RNAPII) coordinates the co-transcriptional recruitment of enzymatic complexes that regulate chromatin states and co-transcriptional processing of nascent RNA. Extensive phosphorylation of serine residues occurs at the structurally-disordered C-terminal domain (CTD) of the largest RNAPII subunit, 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 for the first time mono- and di-methylation of CTD Lysine-7 resid

ORGANISM(S): Mus musculus

SUBMITTER: Elena Torlai Triglia 

PROVIDER: E-GEOD-72876 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress