Transcriptomics

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The C-Terminal Domain of RNA Polymerase II is Modified by Site-Specific Methylation


ABSTRACT: The Carboxy-terminal domain (CTD) of RNA Polymerase II (RNAPII) in mammals undergoes extensive post-translational modification, which is essential for transcriptional initiation and elongation. Here, we show that the CTD of RNAPII is methylated at a single arginine (R1810) by the transcriptional co-activator CARM1. Although methylation at R1810 is present on the hyper-phosphorylated form of RNAPII in vivo, Ser-2 or Ser-5 phosphorylation inhibit CARM1 activity towards this site in vitro, suggesting that methylation occurs before transcription initiation. Mutation of R1810 results in the mis-expression of a variety of snRNAs and snoRNAs, an effect that is also observed in Carm1-/- MEFs. These results demonstrate that CTD methylation facilitates the expression of select RNAs, perhaps serving to discriminate the RNAPII-associated machinery recruited to distinct gene types. To address the function of RNAPII methylation, we generated Raji cell lines expressing an RNA Polymerase II resistant to α-amanitin and carrying either wild-type R1810 or an arginine to alanine substitution at that same residue, abolishing R1810 methylation of the CTD. In cells cultured in α-amanitin, the α-amanitin-resistant mutants fully replaced the functions of endogenous RNAPII, allowing us to study if gene-expression is affected by the absence of R1810me

ORGANISM(S): Homo sapiens  

SUBMITTER: Roberto Bonasio  Danny Reinberg   Robert Sims    

PROVIDER: E-GEOD-27315 | ArrayExpress | 2011-04-01

SECONDARY ACCESSION(S): GSE27315SRP005846PRJNA137181

REPOSITORIES: GEO, ArrayExpress, ENA

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Publications

The C-terminal domain of RNA polymerase II is modified by site-specific methylation.

Sims Robert J RJ   Rojas Luis Alejandro LA   Beck David B DB   Bonasio Roberto R   Schüller Roland R   Drury William J WJ   Eick Dirk D   Reinberg Danny D  

Science (New York, N.Y.) 20110401 6025


The carboxy-terminal domain (CTD) of RNA polymerase II (RNAPII) in mammals undergoes extensive posttranslational modification, which is essential for transcriptional initiation and elongation. Here, we show that the CTD of RNAPII is methylated at a single arginine (R1810) by the coactivator-associated arginine methyltransferase 1 (CARM1). Although methylation at R1810 is present on the hyperphosphorylated form of RNAPII in vivo, Ser2 or Ser5 phosphorylation inhibits CARM1 activity toward this si  ...[more]

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