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Tyrosine-1 and threonine-4 phosphorylation marks complete the RNA polymerase II CTD phospho-code.

RNA Biol. 9, 1144-1146 (2012)
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Open Access Green as soon as Postprint is submitted to ZB.
Eukaryotic RNA polymerase II (RNAP 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 its largest subunit (Rpb1). Dynamic phosphorylation of Ser2, Ser5 and Ser7 residues orchestrates the binding of transcription and RNA processing factors to the transcription machinery. Recent studies show that the two remaining potential phosphorylation sites, tyrosine-1 and threonine-4, are phosphorylated as well and contribute to the previously proposed "CTD code". With the impairment of binding of CTD interacting factors, these novel phosphorylation marks add an accessory layer of regulation to the RNAP II transcription cycle.
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Publication type Article: Journal article
Document type Review
Keywords Transcription ; Rnapii ; Ctd ; Phosphorylation ; Tyr1 ; Thr4; CARBOXY-TERMINAL DOMAIN; TRANSCRIPTION; IICTD
ISSN (print) / ISBN 1547-6286
e-ISSN 1555-8584
Journal RNA Biology
Quellenangaben Volume: 9, Issue: 9, Pages: 1144-1146 Article Number: , Supplement: ,
Publisher Landes Bioscience
Reviewing status Peer reviewed