Evidence map›Paper›PMID 26566685›Full record

ArticleTranscription2015

Site-specific methylation and acetylation of lysine residues in the C-terminal domain (CTD) of RNA polymerase II.

Kirsten Voss, Ignasi Forné, Nicolas Descostes, Corinna Hintermair, Roland Schüller, Muhammad Ahmad Maqbool, Martin Heidemann, Andrew Flatley, Axel Imhof, Marta Gut and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Transcription, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

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  15. The pol II CTD: new twists in the tail.Nature structural & molecular biology · 2016
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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

14 authors at 6 institutions in 3 countries.

Kirsten Vossa Department of Molecular Epigenetics; Helmholtz Center Munich; Center for Integrated Protein Science Munich ; Munich , Germany.
Ignasi Fornéb Biomedical Center Munich; Ludwig Maximilians University Munich ; Planegg-Martinsried , Germany.
Nicolas Descostesc Centre d'Immunologie de Marseille-Luminy; Université Aix-Marseille; Campus de Luminy , France.
Corinna Hintermaira Department of Molecular Epigenetics; Helmholtz Center Munich; Center for Integrated Protein Science Munich ; Munich , Germany.
Roland Schüllera Department of Molecular Epigenetics; Helmholtz Center Munich; Center for Integrated Protein Science Munich ; Munich , Germany.
Muhammad Ahmad Maqboold Institute of Molecular Genetics of Montpellier (IGMM); UMR5535 CNRS ; Montpellier , France.
Martin Heidemanna Department of Molecular Epigenetics; Helmholtz Center Munich; Center for Integrated Protein Science Munich ; Munich , Germany.
Andrew Flatleye Institute of Molecular Immunology; Helmholtz Center Munich ; Munich , Germany.
Axel Imhofc Centre d'Immunologie de Marseille-Luminy; Université Aix-Marseille; Campus de Luminy , France.
Marta Gutf Centre Nacional D'Anàlisi Genòmica; Parc Cientific de Barcelona ; Barcelona , Spain.
Ivo Gutf Centre Nacional D'Anàlisi Genòmica; Parc Cientific de Barcelona ; Barcelona , Spain.
Elisabeth Kremmere Institute of Molecular Immunology; Helmholtz Center Munich ; Munich , Germany.
Jean-Christophe Andraud Institute of Molecular Genetics of Montpellier (IGMM); UMR5535 CNRS ; Montpellier , France.
Dirk Eicka Department of Molecular Epigenetics; Helmholtz Center Munich; Center for Integrated Protein Science Munich ; Munich , Germany.
Helmholtz Zentrum München · DECenter for Integrated Protein Science Munich · DECentre d’Immunologie de Marseille-Luminy · FRCentro Nacional de Análisis Genómico · ESInstitut de Génétique Moléculaire de Montpellier · FRLudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamic modification of heptad-repeats with the consensus sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 of RNA polymerase II (RNAPII) C-terminal domain (CTD) regulates transcription-coupled processes. Mass spectrometry analysis revealed that K7-residues in non-consensus repeats of human RNAPII are modified by acetylation, or mono-, di-, and tri-methylation. K7ac, K7me2, and K7me3 were found exclusively associated with phosphorylated CTD peptides, while K7me1 occurred also in non-phosphorylated CTD. The monoclonal antibody 1F5 recognizes K7me1/2 residues in CTD and reacts with RNAPIIA. Treatment of cellular extracts with phosphatase or of cells with the kinase inhibitor flavopiridol unmasked the K7me1/2 epitope in RNAPII0, consistent with the association of K7me1/2 marks with phosphorylated CTD peptides. Genome-wide profiling revealed high levels of K7me1/2 marks at the transcriptional start site of genes for sense and antisense transcribing RNAPII. The new K7 modifications further expand the mammalian CTD code to allow regulation of differential gene expression.

Indexed as

AcetylationAntibodies, MonoclonalCell LineGene Expression RegulationHumansLysineMass SpectrometryMethylationModels, MolecularProtein Structure, TertiaryRNA Polymerase IITranscription Initiation, GeneticAntibodies, MonoclonalLysineRNA Polymerase IICTD codeC-terminal domain (CTD)lysine methylationRNA polymerase II

Identifiers

PMID26566685
PMCPMC4802791
OpenAlexW2251091162

What Socratic 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 Socratic graph.