Evidence map›Paper›PMID 31054975›Full record

ArticleMolecular cell2019

Crosstalk between RNA Pol II C-Terminal Domain Acetylation and Phosphorylation via RPRD Proteins.

Ibraheem Ali, Diego Garrido Ruiz, Zuyao Ni, Jeffrey R Johnson, Heng Zhang, Pao-Chen Li, Mir M Khalid, Ryan J Conrad, Xinghua Guo, Jinrong Min and 4 more

Abstract read
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. An Important Role for RPRD1B in the Heat Shock Response.Molecular and cellular biology · 2022
    Article
  14. Review
  15. The HDAC inhibitor CI-994 acts as a molecular memory aid by facilitating synaptic and intracellular communication after learning.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review
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.

Ibraheem AliJ. David Gladstone Institutes, San Francisco, CA 94158, USA; Department of Medicine, University of California San Francisco, San Francisco, CA 94143, USA.
Diego Garrido RuizDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA.
Zuyao NiDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Jeffrey R JohnsonJ. David Gladstone Institutes, San Francisco, CA 94158, USA.
Heng ZhangStructural Genomics Consortium, University of Toronto, ON, Canada.
Pao-Chen LiJ. David Gladstone Institutes, San Francisco, CA 94158, USA.
Mir M KhalidJ. David Gladstone Institutes, San Francisco, CA 94158, USA.
Ryan J ConradJ. David Gladstone Institutes, San Francisco, CA 94158, USA; Department of Medicine, University of California San Francisco, San Francisco, CA 94143, USA.
Xinghua GuoDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Jinrong MinStructural Genomics Consortium, University of Toronto, ON, Canada.
Jack GreenblattDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Matthew JacobsonDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA; California Institute for Quantitative Biosciences (QBC), University of California, San Francisco, San Francisco, CA 94143, USA.
Nevan J KroganJ. David Gladstone Institutes, San Francisco, CA 94158, USA; California Institute for Quantitative Biosciences (QBC), University of California, San Francisco, San Francisco, CA 94143, USA.
Melanie OttJ. David Gladstone Institutes, San Francisco, CA 94158, USA; Department of Medicine, University of California San Francisco, San Francisco, CA 94143, USA. Electronic address: melanie.ott@gladstone.ucsf.edu.

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KROGAN, NEVAN J · 2007 to 2018
$48.8M
MOLECULAR AND CELLULAR IMMUNOLOGYT32AI007334 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CYSTER, JASON G · 1988 to 2023
$11.0M
Virology CoreP01CA177322 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WU, TING-TING · 2014 to 2018
$8.7M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Role of Factor Acetylation in the Regulation of HIV TranscriptionR37AI083139 · NIAID · J. DAVID GLADSTONE INSTITUTES · PI Melanie Maria Ott · 2019 to 2026
$5.5M
Role of Factor Acetylation in the Regulation of HIV TranscriptionR01AI083139 · NIAID · J. DAVID GLADSTONE INSTITUTES · PI OTT, MELANIE MARIA · 2009 to 2017
$3.9M
Targeting lysine methylation for latency reversal in HIV-infected drug usersR01DA043142 · NIDA · J. DAVID GLADSTONE INSTITUTES · PI OTT, MELANIE MARIA · 2016 to 2020
$3.0M
NCI NIH HHS P01 CA177322NIAID NIH HHS R01 AI083139NIAID NIH HHS R37 AI083139NIAID NIH HHS T32 AI007334NIDA NIH HHS R01 DA043142NIGMS NIH HHS P41 GM103311NIGMS NIH HHS P50 GM082250
6 · The paper itself

Abstract

Post-translational modifications of the RNA polymerase II C-terminal domain (CTD) coordinate the transcription cycle. Crosstalk between different modifications is poorly understood. Here, we show how acetylation of lysine residues at position 7 of characteristic heptad repeats (K7ac)-only found in higher eukaryotes-regulates phosphorylation of serines at position 5 (S5p), a conserved mark of polymerases initiating transcription. We identified the regulator of pre-mRNA-domain-containing (RPRD) proteins as reader proteins of K7ac. K7ac enhanced CTD peptide binding to the CTD-interacting domain (CID) of RPRD1A and RPRD1B proteins in isothermal calorimetry and molecular modeling experiments. Deacetylase inhibitors increased K7ac- and decreased S5-phosphorylated polymerases, consistent with acetylation-dependent S5 dephosphorylation by an RPRD-associated S5 phosphatase. Consistent with this model, RPRD1B knockdown increased S5p but enhanced K7ac, indicating that RPRD proteins recruit K7 deacetylases, including HDAC1. We also report autoregulatory crosstalk between K7ac and S5p via RPRD proteins and their interactions with acetyl- and phospho-eraser proteins.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceAnimalsBinding SitesCell Cycle ProteinsHEK293 CellsHumansMiceModels, MolecularNeoplasm ProteinsNIH 3T3 CellsPhosphorylationProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandCell Cycle ProteinsNeoplasm ProteinsProtein IsoformsRNA Polymerase IIRNA, Small InterferingRPRD1B protein, humanacetylationcrosstalkC-terminal domaingene regulationhistone deacetylasephosphorylationPol II CTDpost-translational modificationRNA polymerase IItranscription

Identifiers

PMID31054975
PMCPMC6588463

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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.