Evidence map›Paper›PMID 26799764›Full record

ArticleMolecular cell2016

Direct Analysis of Phosphorylation Sites on the Rpb1 C-Terminal Domain of RNA Polymerase II.

Hyunsuk Suh, Scott B Ficarro, Un-Beom Kang, Yujin Chun, Jarrod A Marto, Stephen Buratowski

Abstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

77 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
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  5. Leveraging HILIC/ERLIC separations for online nanoscale LC-MS/MS analysis of phosphopeptide isoforms from RNA polymerase II C-terminal domain.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2025
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  17. Mediator and Pol II go to eleven (CTD repeats).Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Review
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17 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Hyunsuk SuhDepartment of Biochemical Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Cancer Biology and Blais Proteomics Center, Dana Farber Cancer Institute, Boston, MA 02115, USA.
Scott B FicarroDepartment of Biochemical Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Cancer Biology and Blais Proteomics Center, Dana Farber Cancer Institute, Boston, MA 02115, USA.
Un-Beom KangDepartment of Biochemical Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Cancer Biology and Blais Proteomics Center, Dana Farber Cancer Institute, Boston, MA 02115, USA.
Yujin ChunDepartment of Biochemical Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Jarrod A MartoDepartment of Biochemical Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Cancer Biology and Blais Proteomics Center, Dana Farber Cancer Institute, Boston, MA 02115, USA.
Stephen BuratowskiDepartment of Biochemical Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: steveb@hms.harvard.edu.
Harvard University · US

Funding

The RNA Polymerase II Transcription CycleR01GM056663 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Stephen Buratowski · 1999 to 2026
$11.7M
NIGMS NIH HHS GM56663NIGMS NIH HHS R01 GM056663
6 · The paper itself

Abstract

Dynamic interactions between RNA polymerase II and various mRNA-processing and chromatin-modifying enzymes are mediated by the changing phosphorylation pattern on the C-terminal domain (CTD) of polymerase subunit Rpb1 during different stages of transcription. Phosphorylations within the repetitive heptamer sequence (YSPTSPS) of CTD have primarily been defined using antibodies, but these do not distinguish different repeats or allow comparative quantitation. Using a CTD modified for mass spectrometry (msCTD), we show that Ser5-P and Ser2-P occur throughout the length of CTD and are far more abundant than other phosphorylation sites. msCTD extracted from cells mutated in several CTD kinases or phosphatases showed the expected changes in phosphorylation. Furthermore, msCTD associated with capping enzyme was enriched for Ser5-P while that bound to the transcription termination factor Rtt103 had higher levels of Ser2-P. These results suggest a relatively sparse and simple "CTD code."

Indexed as

Amino Acid SequenceCell ProliferationMass SpectrometryMolecular Sequence DataMutationPhosphorylationProtein Structure, TertiaryRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticRNA Polymerase IIRPB1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID26799764
PMCPMC4724063
OpenAlexW2289132128

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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.