RPRD1A and RPRD1B Are Human RNA Polymerase II C-Terminal Domain Scaffolds for Ser5 Dephosphorylation

@article{Ni2014RPRD1AAR,
  title={RPRD1A and RPRD1B Are Human RNA Polymerase II C-Terminal Domain Scaffolds for Ser5 Dephosphorylation},
  author={Zuyao Ni and Chao Xu and Xinghua Guo and Gerald O. Hunter and Olga V. Kuznetsova and Wolfram Tempel and Edyta Marcon and Guoqing Zhong and Hongbo Guo and Wei-Hung William Kuo and Joyce Li and Peter Young and Jonathan B. Olsen and Cuihong Wan and Peter Loppnau and Majida El Bakkouri and Guillermo A. Senisterra and Hao He and Haiming Huang and Sachdev S. Sidhu and Andrew Emili and Shona Murphy and A. Mosley and Cheryl H. Arrowsmith and Jinrong Min and Jack F Greenblatt},
  journal={Nature structural \& molecular biology},
  year={2014},
  volume={21},
  pages={686 - 695}
}
The RNA polymerase II (RNAPII) C-terminal domain (CTD) heptapeptide repeats (1-YSPTSPS-7) undergo dynamic phosphorylation and dephosphorylation during the transcription cycle to recruit factors that regulate transcription, RNA processing and chromatin modification. We show here that RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Crystal… 
Phosphatase Rtr1 Regulates Global Levels of Serine 5 RNA Polymerase II C-Terminal Domain Phosphorylation and Cotranscriptional Histone Methylation
TLDR
Findings suggest that Rtr1 regulates H3K36me3 levels through changes in the number of binding sites for the histone methyltransferase Set2, thereby influencing both the CTD and histone codes.
Human RNA polymerase II-associated protein 2 (RPAP2) interacts directly with the RNA polymerase II subunit Rpb6 and participates in pre-mRNA 3'-end formation.
TLDR
It is demonstrated that the C-terminal region of RPAP2 interacts directly with the Pol II subunit Rpb6 and participates in pre-mRNA 3'-end formation.
Crosstalk between RNA Pol II C-Terminal Domain Acetylation and Phosphorylation via RPRD Proteins.
Crosstalk between RNA Pol II C-Terminal Domain Acetylation and Phosphorylation via RPRD Proteins
TLDR
It is shown how acetylation of lysine residues at position 7 of characteristic heptad repeats (K7ac), a modification only found in higher eukaryotes, regulates phosphorylation of serines at position 5 (S5p), a conserved mark of polymerases initiating transcription.
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TLDR
The solution structure of the Rtt103p CTD‐interacting domain (CID) bound to Thr4 phosphorylated CTD reveals a direct recognition of the phospho‐Thr4 mark by Rtt 103p CID and extensive interactions involving residues from three repeats of the CTD heptad, suggesting that the recruitment of a CID‐containing CTd‐binding factor may be coded by more than one letter of theCTD code.
Different phosphoisoforms of RNA polymerase II engage the Rtt103 termination factor in a structurally analogous manner
TLDR
A role for phospho-Thr4 in transcription termination at noncoding small nucleolar RNA (snoRNA) genes is identified and an interactome of known readers as well as protein complexes that were not known to rely on Thr4 for association with Pol II is revealed.
An Investigation of the Regulation of RNA Polymerase II Transcription Termination by SMN, FUS, and TDP-43 in a pathway involving Symmetric Arginine Dimethylation (R1810) of the RNAPII CTD
TLDR
It is proposed that mis-regulation of RNAPII termination could lead to DNA damage, which may contribute to neurodegenerative disorders like SMA and ALS/FTD.
Current understanding of CREPT and p15RS, carboxy-terminal domain (CTD)-interacting proteins, in human cancers
TLDR
Fully revealing the mechanisms of CREPT and p15RS functions will not only provide new insights into understanding gene transcription and maintenance of DNA stability in tumors, but also promote new approach development for tumor diagnosis and therapy.
RNA Polymerase II CTD phosphatase Rtr1 prevents premature transcription termination
TLDR
A new role is defined for the phosphatase Rtr1 in the regulation of RNA Polymerase II progression from the start of transcription to the 3’ end of the gene where the nascent RNA from protein-coding genes is typically cleaved and polyadenylated.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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