Journal
EMBO JOURNAL
Volume 31, Issue 12, Pages 2784-2797Publisher
WILEY
DOI: 10.1038/emboj.2012.123
Keywords
elongation; phosphorylation; Plk3; Pol II CTD; threonine-4
Categories
Funding
- Deutsche Forschungsgemeinschaft [SFB-Transregio5, SFB684]
- Institut National de la Sante et de la Recherche Medicale
- Centre National de la Recherche Scientifique (CNRS)
- Fondation Princesse Grace de Monaco
- Agence Nationale de la Recherche (ANR)
- Institut National du Cancer (INCa)
- Commission of the European Communities
- 'Chromatin Plasticity' Marie Curie Research Training Network Association pour la Recherche sur le Cancer and Agence Nationale de la recherche (ANR 'ChromaTin') [MRTN-CT-2006-0357733]
- Genopole
- Fondation pour la Recherche Medicale
- ESGI consortium grant of the EU
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Eukaryotic RNA polymerase II (Pol II) has evolved an array of heptad repeats with the consensus sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 at the carboxy-terminal domain (CTD) of the large subunit (Rpb1). Differential phosphorylation of Ser2, Ser5, and Ser7 in the 5' and 3' regions of genes coordinates the binding of transcription and RNA processing factors to the initiating and elongating polymerase complexes. Here, we report phosphorylation of Thr4 by Polo-like kinase 3 in mammalian cells. ChIPseq analyses indicate an increase of Thr4-P levels in the 3' region of genes occurring subsequently to an increase of Ser2-P levels. A Thr4/Ala mutant of Pol II displays a lethal phenotype. This mutant reveals a global defect in RNA elongation, while initiation is largely unaffected. Since Thr4 replacement mutants are viable in yeast we conclude that this amino acid has evolved an essential function(s) in the CTD of Pol II for gene transcription in mammalian cells. The EMBO Journal (2012) 31, 2784-2797. doi:10.1038/emboj.2012.123; Published online 1 May 2012
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