Evidence map›Paper›PMID 26217014›Full record

ArticleMolecular and cellular biology2015

Characterization of the Human Transcription Elongation Factor Rtf1: Evidence for Nonoverlapping Functions of Rtf1 and the Paf1 Complex.

Qing-Fu Cao, Junichi Yamamoto, Tomoyasu Isobe, Shumpei Tateno, Yuki Murase, Yexi Chen, Hiroshi Handa, Yuki Yamaguchi

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.5field-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

36 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Kinetic control of mammalian transcription elongation.Nature structural & molecular biology · 2026
    Article
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  11. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Rtf1 Transcriptionally Regulates Neonatal and Adult Cardiomyocyte Biology.Journal of cardiovascular development and disease · 2023
    Article
  18. Article
  19. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Qing-Fu CaoGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Junichi YamamotoGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Tomoyasu IsobeGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Shumpei TatenoGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Yuki MuraseGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Yexi ChenGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Hiroshi HandaDepartment of Nanoparticle Translational Research, Tokyo Medical University, Tokyo, Japan.
Yuki YamaguchiGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan yyamaguc@bio.titech.ac.jp.
Tokyo Institute of Technology · JPTokyo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Restores TBP function 1 (Rtf1) is generally considered to be a subunit of the Paf1 complex (PAF1C), a multifunctional protein complex involved in histone modification and transcriptional or posttranscriptional regulation. Rtf1, however, is not stably associated with the PAF1C in most species except Saccharomyces cerevisiae, and its biochemical functions are not well understood. Here, we show that human Rtf1 is a transcription elongation factor that may function independently of the PAF1C. Rtf1 requires "Rtf1 coactivator" activity, which is most likely unrelated to the PAF1C or DSIF, for transcriptional activation in vitro. A mutational study revealed that the Plus3 domain of human Rtf1 is critical for its coactivator-dependent function. Transcriptome sequencing (RNA-seq) and chromatin immunoprecipitation studies in HeLa cells showed that Rtf1 and the PAF1C play distinct roles in regulating the expression of a subset of genes. Moreover, contrary to the finding in S. cerevisiae, the PAF1C was apparently recruited to the genes examined in an Rtf1-independent manner. The present study establishes a role for human Rtf1 as a transcription elongation factor and highlights the similarities and differences between the S. cerevisiae and human Rtf1 proteins.

Indexed as

Gene OntologyHeLa CellsHumansNuclear ProteinsTranscriptional ActivationTranscription Elongation, GeneticTranscription FactorsUbiquitinationNuclear ProteinsPAF1 protein, humanRTF1 protein, humanTranscription Factors

Identifiers

PMID26217014
PMCPMC4573716
OpenAlexW2230596985

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.