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• W2013286714 endingPage "226" @default.
• W2013286714 startingPage "223" @default.
• W2013286714 abstract "During transcription, RNA polymerase (Pol) II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing by the carboxy-terminal domain (CTD) of Pol II, which consists of up to 52 repeats of the sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 (refs 1, 2). After phosphorylation, the CTD binds tightly to a conserved CTD-interacting domain (CID) present in the proteins Pcf11 and Nrd1, which are essential and evolutionarily conserved factors for polyadenylation-dependent and -independent 3'-RNA processing, respectively. Here we describe the structure of a Ser 2-phosphorylated CTD peptide bound to the CID domain of Pcf11. The CTD motif Ser 2-Pro 3-Thr 4-Ser 5 forms a beta-turn that binds to a conserved groove in the CID domain. The Ser 2 phosphate group does not make direct contact with the CID domain, but may be recognized indirectly because it stabilizes the beta-turn with an additional hydrogen bond. Iteration of the peptide structure results in a compact beta-spiral model of the CTD. The model suggests that, during the mRNA transcription-processing cycle, compact spiral regions in the CTD are unravelled and regenerated in a phosphorylation-dependent manner." @default.
• W2013286714 created "2016-06-24" @default.
• W2013286714 creator A5008281609 @default.
• W2013286714 creator A5039624302 @default.
• W2013286714 date "2004-07-01" @default.
• W2013286714 modified "2023-10-05" @default.
• W2013286714 title "Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors" @default.
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• W2013286714 doi "https://doi.org/10.1038/nature02679" @default.
• W2013286714 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15241417" @default.
• W2013286714 hasPublicationYear "2004" @default.
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