Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors
@article{Meinhart2004RecognitionOR, title={Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors}, author={Anton Meinhart and Patrick Cramer}, journal={Nature}, year={2004}, volume={430}, pages={223-226} }
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…
324 Citations
Role of the RNA polymerase II C-terminal domain in transcription termination and function of Spt5 in 3' RNA-processing factor recruitment.
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Two new aspects of transcription and RNA processing regulation by two different C-terminal repetitive protein domains are characterized, including a new role of the Spt5 CTR in recruitment of RNA 3’-end processing factors.
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The ability to separate phosphorylated and unphosphorylated CTD species by SDS gel electrophoresis has allowed the characterization of CTD phosphorylation states established both in vitro and in vivo.
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Evidence is provided for the binding of two Zn2+ atoms to Pcf11, bound to separate zinc-binding domains located on each side of the Clp1 recognition region that contribute to a more complete understanding of the architecture and function of Pcf 11 and its role within the yeast CF IA complex.
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TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II.
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Phosphoserines of the carboxy terminal domain of RNA polymerase II are involved in the interaction with transcription-associated proteins (TAPs).
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Among the different phosphorylated forms of CTD, the form found to have the most affinity for a particular protein was also the form that is predominant during that process, the only exception being the equally high affinity of S2P CTD to Spt4, although S5PCTD is the known active form during elongation.
The RNA polymerase II CTD coordinates transcription and RNA processing.
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Findings regarding modification and function of the C-terminal domain are reviewed, highlighting the important role this unique domain plays in coordinating gene activity.
RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc 7
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- 2014
This work shows that Glc7 is a Tyr1 phosphatase both in vitro and in vivo and investigates the role of CPF in CTD phosphorylation, which is proposed to have a role in 3′-end processing.
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