Evidence map›Paper›PMID 19394294›Full record

ArticleMolecular cell2009

Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation.

Amber L Mosley, Samantha G Pattenden, Michael Carey, Swaminathan Venkatesh, Joshua M Gilmore, Laurence Florens, Jerry L Workman, Michael P Washburn

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

84 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. RNA Pol II Assembly Affects ncRNA Expression.International journal of molecular sciences · 2023
    Article
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  7. Article
  8. Review
  9. Article
  10. Histone sumoylation and chromatin dynamics.Nucleic acids research · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021
    Review
  15. Proteome analysis ofBiochemistry and biophysics reports · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

24 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Amber L MosleyStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Samantha G Pattenden
Michael Carey
Swaminathan Venkatesh
Joshua M Gilmore
Laurence Florens
Jerry L Workman
Michael P Washburn
Stowers Institute for Medical Research · US

Funding

Dynamics of mRNA Elongation Regulatory ComplexesF32GM075541 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI MOSLEY, AMBER LEE · 2005 to 2007
$143k
NIGMS NIH HHS F32 GM 075541NIGMS NIH HHS F32 GM075541
6 · The paper itself

Abstract

Messenger RNA processing is coupled to RNA polymerase II (RNAPII) transcription through coordinated recruitment of accessory proteins to the Rpb1 C-terminal domain (CTD). Dynamic changes in CTD phosphorylation during transcription elongation are responsible for their recruitment, with serine 5 phosphorylation (S5-P) occurring toward the 5' end of genes and serine 2 phosphorylation (S2-P) occurring toward the 3' end. The proteins responsible for regulation of the transition state between S5-P and S2-P CTD remain elusive. We show that a conserved protein of unknown function, Rtr1, localizes within coding regions, with maximum levels of enrichment occurring between the peaks of S5-P and S2-P RNAPII. Upon deletion of Rtr1, the S5-P form of RNAPII accumulates in both whole-cell extracts and throughout coding regions; additionally, RNAPII transcription is decreased, and termination defects are observed. Functional characterization of Rtr1 reveals its role as a CTD phosphatase essential for the S5-to-S2-P transition.

Indexed as

Chromatin ImmunoprecipitationModels, GeneticOpen Reading FramesPhosphoprotein PhosphatasesPhosphorylationProtein Interaction MappingProton-Translocating ATPasesRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSerineTranscription FactorsTranscription, Geneticcarboxy-terminal domain phosphatasePhosphoprotein PhosphatasesPMA1 protein, S cerevisiaeProton-Translocating ATPasesRNA Polymerase IIRtr1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerineTranscription Factors

Identifiers

PMID19394294
PMCPMC2996052
OpenAlexW1966695149

What OpenQuestion holds

Textmetadata
LicenceTDM
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.