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… 

Figures from this paper

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TLDR
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TLDR
It is shown that the human RNA processing factor SCAF8 interacts weakly with the unphosphorylated CTD of Pol II, and motifs within CIDs that are involved in a generic CTD sequence recognition are distinguished from items that confer phospho-specificity.
RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.
TLDR
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.
Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3′-end processing
TLDR
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.
Phosphoserines of the carboxy terminal domain of RNA polymerase II are involved in the interaction with transcription-associated proteins (TAPs).
TLDR
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.
TLDR
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
TLDR
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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TLDR
It is shown that read-through transcription from yeast small nucleolar RNA and small nuclear RNA genes into adjacent genes is prevented by a cis-acting element that is recognized, in part, by the essential RNA-binding protein Nrd1.
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TLDR
Data reinforce the concept that CTD phosphorylation acts as a regulatory mechanism in the maturation of the primary transcript by establishing a direct interaction of cleavage/polyadenylation factor IA with the CTD.
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TLDR
The results suggest that the CTD and a set of CTD-binding proteins may act to physically and functionally link transcription and pre-mRNA processing.
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A dynamic association of mRNA processing factors with differently modified forms of the polymerase throughout the transcription cycle is suggested.
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TLDR
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