Evidence map›Paper›PMID 24196955›Full record

ArticleThe Journal of biological chemistry2013

The RNA polymerase II C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome.

Dong-hyuk Heo, Inhea Yoo, Jiwon Kong, Michael Lidschreiber, Andreas Mayer, Byung-Yi Choi, Yoonsoo Hahn, Patrick Cramer, Stephen Buratowski, Minkyu Kim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Polyadenylated versions of small non-coding RNAs inMicrobial cell (Graz, Austria) · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Aep3p-dependent translation of yeast mitochondrialMolecular biology of the cell · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 3 countries.

Dong-hyuk HeoFrom the Center for RNA Research, Institute for Basic Science and.
Inhea Yoo
Jiwon Kong
Michael Lidschreiber
Andreas Mayer
Byung-Yi Choi
Yoonsoo Hahn
Patrick Cramer
Stephen Buratowski
Minkyu Kim
Institute for Basic Science · KRLudwig-Maximilians-Universität München · DESeoul National University · KRChung-Ang University · KRHarvard University · US

Funding

The RNA Polymerase II Transcription CycleR01GM056663 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Stephen Buratowski · 1999 to 2026
$11.7M
NIGMS NIH HHS GM56663NIGMS NIH HHS R01 GM056663
6 · The paper itself

Abstract

The RNA polymerase II (RNApII) C-terminal domain (CTD)-interacting domain (CID) proteins are involved in two distinct RNApII termination pathways and recognize different phosphorylated forms of CTD. To investigate the role of differential CTD-CID interactions in the choice of termination pathway, we altered the CTD-binding specificity of Nrd1 by domain swapping. Nrd1 with the CID from Rtt103 (Nrd1(CID(Rtt103))) causes read-through transcription at many genes, but can also trigger termination where multiple Nrd1/Nab3-binding sites and the Ser(P)-2 CTD co-exist. Therefore, CTD-CID interactions target specific termination complexes to help choose an RNApII termination pathway. Interactions of Nrd1 with both CTD and nascent transcripts contribute to efficient termination by the Nrd1 complex. Surprisingly, replacing the Nrd1 CID with that from Rtt103 reduces binding to Rrp6/Trf4, and RNA transcripts terminated by Nrd1(CID(Rtt103)) are predominantly processed by core exosome. Thus, the Nrd1 CID couples Ser(P)-5 CTD not only to termination, but also to RNA processing by the nuclear exosome.

Indexed as

RNA Processing, Post-TranscriptionalTranscription Termination, GeneticAlcohol DehydrogenaseBase SequenceBinding SitesCell NucleusExosome Multienzyme Ribonuclease ComplexMolecular Sequence DataMutationNuclear ProteinsProtein Structure, TertiaryRNA-Binding ProteinsRNA, MessengerRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsADH1 protein, S cerevisiaeAlcohol DehydrogenaseExosome Multienzyme Ribonuclease ComplexNAB3 protein, S cerevisiaeNRD1 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsRNA, MessengerRNA Polymerase IIRRP6 protein, S cerevisiaeRtt103 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsC-terminal DomainmRNANrd1RNA Polymerase IIRNA ProcessingSmall Nucleolar RNA (snoRNA)Transcription Termination

Identifiers

PMID24196955
PMCPMC3868778
OpenAlexW2048858964

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.