Evidence map›Paper›PMID 25575120›Full record

ArticleNature communications2015

MED26 regulates the transcription of snRNA genes through the recruitment of little elongation complex.

Hidehisa Takahashi, Ichigaku Takigawa, Masashi Watanabe, Delnur Anwar, Mio Shibata, Chieri Tomomori-Sato, Shigeo Sato, Amol Ranjan, Chris W Seidel, Tadasuke Tsukiyama and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  5. Review
  6. SUMO conjugation to promoter-proximal sequence elements-associated proteins impacts on snRNA transcription.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

16 authors at 4 institutions in 2 countries.

Hidehisa TakahashiDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Ichigaku TakigawaCreative Research Institution, Hokkaido University, Kita 21, Nishi 10, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Masashi WatanabeDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Delnur AnwarDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Mio ShibataDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Chieri Tomomori-SatoStowers Institute for Medical Research, 1000 E, 50th Street, Kansas City, Missouri 64110, USA.
Shigeo SatoStowers Institute for Medical Research, 1000 E, 50th Street, Kansas City, Missouri 64110, USA.
Amol RanjanStowers Institute for Medical Research, 1000 E, 50th Street, Kansas City, Missouri 64110, USA.
Chris W SeidelStowers Institute for Medical Research, 1000 E, 50th Street, Kansas City, Missouri 64110, USA.
Tadasuke TsukiyamaDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Wataru MizushimaDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Masayasu HayashiDepartment of Advanced Medical Initiatives, Kyushu University Graduate School of Medical Sciences, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
Yasuyuki OhkawaDepartment of Advanced Medical Initiatives, Kyushu University Graduate School of Medical Sciences, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
Joan W Conaway1] Stowers Institute for Medical Research, 1000 E, 50th Street, Kansas City, Missouri 64110, USA [2] Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City KS 66160, USA.
Ronald C Conaway1] Stowers Institute for Medical Research, 1000 E, 50th Street, Kansas City, Missouri 64110, USA [2] Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City KS 66160, USA.
Shigetsugu HatakeyamaDepartment of Biochemistry, Hokkaido University Graduate School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.
Hokkaido University · JPStowers Institute for Medical Research · USKyushu University · JPUniversity of Kansas Medical Center · US

Funding

BIOCHEMISTRY OF EUKARYOTIC MESSENGER RNA SYNTHESISR37GM041628 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI CONAWAY, RONALD C. · 2000 to 2009
$3.8M
BIOCHEMISTRY OF EUKARYOTIC MESSENGER SYNTHESISR01GM041628 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI CONAWAY, JOAN W, CONAWAY, RONALD C. · 1989 to 2013
$1.5M
NIGMS NIH HHS GM41628NIGMS NIH HHS R01 GM041628NIGMS NIH HHS R37 GM041628
6 · The paper itself

Abstract

Regulation of transcription elongation by RNA polymerase II (Pol II) is a key regulatory step in gene transcription. Recently, the little elongation complex (LEC)-which contains the transcription elongation factor ELL/EAF-was found to be required for the transcription of Pol II-dependent small nuclear RNA (snRNA) genes. Here we show that the human Mediator subunit MED26 plays a role in the recruitment of LEC to a subset of snRNA genes through direct interaction of EAF and the N-terminal domain (NTD) of MED26. Loss of MED26 in cells decreases the occupancy of LEC at a subset of snRNA genes and results in a reduction in their transcription. Our results suggest that the MED26-NTD functions as a molecular switch in the exchange of TBP-associated factor 7 (TAF7) for LEC to facilitate the transition from initiation to elongation during transcription of a subset of snRNA genes.

Indexed as

Peptide Chain Elongation, TranslationalTranscription, GeneticAmino Acid SequenceAnimalsDNA Polymerase IIFibroblastsHEK293 CellsHeLa CellsHumansMediator ComplexMiceMice, Inbred C57BLMolecular Sequence DataPoint MutationProtein BindingRecombinant ProteinsDNA Polymerase IIEAF1 protein, humanMED26 protein, humanMediator ComplexRecombinant ProteinsRNA, Small NuclearTAF7 protein, humanTATA-Binding Protein Associated FactorsTranscription FactorsTranscription Factor TFIID

Identifiers

PMID25575120
PMCPMC4646223
OpenAlexW2041348350

What OpenQuestion holds

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Registered trials

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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.