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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Threonine-4 of mammalian RNA polymerase II CTD is targeted by Polo-like kinase 3 and required for transcriptional elongation.
EMBO J. 31, 2784-2797 (2012)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Elongation; Phosphorylation; Plk3; Pol Ii Ctd; Threonine-4; C-TERMINAL DOMAIN; EXPORT FACTOR YRA1; CELL-PROLIFERATION; GENE-EXPRESSION; LARGE SUBUNIT; TFIIH KINASE; PHOSPHORYLATION; COMPLEX; PHOSPHATASE; IICTD
ISSN (print) / ISBN
0261-4189
e-ISSN
1460-2075
Journal
EMBO Journal, The
Quellenangaben
Volume: 31,
Issue: 12,
Pages: 2784-2797
Publisher
Wiley
Publishing Place
Heidelberg, Germany
Reviewing status
Peer reviewed