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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)
Verlagsversion Volltext DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Transcription ; Rnapii ; Ctd ; Phosphorylation ; Tyr1 ; Thr4; CARBOXY-TERMINAL DOMAIN; TRANSCRIPTION; IICTD
ISSN (print) / ISBN 1547-6286
e-ISSN 1555-8584
Zeitschrift RNA Biology
Quellenangaben Band: 9, Heft: 9, Seiten: 1144-1146 Artikelnummer: , Supplement: ,
Verlag Landes Bioscience
Begutachtungsstatus