Evidence map›Paper›PMID 25416796›Full record

ArticleNucleic acids research2014

Rpb4/7 facilitates RNA polymerase II CTD dephosphorylation.

Paula Allepuz-Fuster, Verónica Martínez-Fernández, Ana I Garrido-Godino, Sergio Alonso-Aguado, Steven D Hanes, Francisco Navarro, Olga Calvo

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  8. The Role ofCells · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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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

7 authors at 3 institutions in 2 countries.

Paula Allepuz-Fuster
Verónica Martínez-Fernández
Ana I Garrido-Godino
Sergio Alonso-Aguado
Steven D Hanes
Francisco Navarro
Olga Calvo
Instituto de Biología Funcional y Genómica · ESUniversidad de Jaén · ESSUNY Upstate Medical University · US

Funding

Yeast Ess1, a Conserved PPlase Essential for MitosisR01GM055108 · NIGMS · WADSWORTH CENTER · PI HANES, STEVEN D. · 1997 to 2010
$2.5M
NIGMS NIH HHS R01-GM055108
6 · The paper itself

Abstract

The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAPII) participate in a variety of processes from transcription, DNA repair, mRNA export and decay, to translation regulation and stress response. However, their mechanism(s) of action remains unclear. Here, we show that the Rpb4/7 heterodimer in Saccharomyces cerevisiae plays a key role in controlling phosphorylation of the carboxy terminal domain (CTD) of the Rpb1 subunit of RNAPII. Proper phosphorylation of the CTD is critical for the synthesis and processing of RNAPII transcripts. Deletion of RPB4, and mutations that disrupt the integrity of Rpb4/7 or its recruitment to the RNAPII complex, increased phosphorylation of Ser2, Ser5, Ser7 and Thr4 within the CTD. RPB4 interacted genetically with genes encoding CTD phosphatases (SSU72, FCP1), CTD kinases (KIN28, CTK1, SRB10) and a prolyl isomerase that targets the CTD (ESS1). We show that Rpb4 is important for Ssu72 and Fcp1 phosphatases association, recruitment and/or accessibility to the CTD, and that this correlates strongly with Ser5P and Ser2P levels, respectively. Our data also suggest that Fcp1 is the Thr4P phosphatase in yeast. Based on these and other results, we suggest a model in which Rpb4/7 helps recruit and potentially stimulate the activity of CTD-modifying enzymes, a role that is central to RNAPII function.

Indexed as

Cyclin-Dependent KinasesmRNA Cleavage and Polyadenylation FactorsMutationNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoprotein PhosphatasesProtein KinasesProtein MultimerizationProtein Structure, TertiaryRNA Polymerase IISaccharomyces cerevisiae Proteinscarboxy-terminal domain phosphataseCTDK-I protein complex, S cerevisiaeCyclin-Dependent KinasesESS1 protein, S cerevisiaeKin28 protein kinase, S cerevisiaemRNA Cleavage and Polyadenylation FactorsNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoprotein PhosphatasesProtein KinasesRNA Polymerase IIRPB1 protein, S cerevisiaeRPB4 protein, S cerevisiaeRPB7 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSSU72 protein, S cerevisiae

Identifiers

PMID25416796
PMCPMC4267648
OpenAlexW2065136241

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.