Evidence map›Paper›PMID 30169671›Full record

ArticleNucleic acids research2018

Identification of the RNA polymerase I-RNA interactome.

David Piñeiro, Mark Stoneley, Manasa Ramakrishna, Jana Alexandrova, Veronica Dezi, Rebekha Juke-Jones, Kathryn S Lilley, Kelvin Cain, Anne E Willis

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. 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
1.4field-weighted citation impact, top 18% 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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  13. The primary mechanism of cytotoxicity of the chemotherapeutic agent CX-5461 is topoisomerase II poisoning.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. The peculiar genetics of the ribosomal DNA blurs the boundaries of transgenerational epigenetic inheritance.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2019
    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

9 authors at 2 institutions in 1 country.

David PiñeiroMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Mark StoneleyMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Manasa RamakrishnaMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Jana AlexandrovaMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Veronica DeziMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Rebekha Juke-JonesMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Kathryn S LilleyCambridge Centre for Proteomics, University of Cambridge, Department of Biochemistry, Tennis Court Road, Cambridge CB2 1QR, UK.
Kelvin CainMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Anne E WillisMedical Research Council Toxicology Unit, University of Cambridge, Lancaster Rd, Leicester LE1 9HN, UK.
Medical Research Council · GBUniversity of Cambridge · GB

Funding

Medical Research Council MC_UP_A600_1023Medical Research Council MC_UU_00025/7Wellcome Trust 110170/Z/15/Z
6 · The paper itself

Abstract

Ribosome biogenesis is a complex process orchestrated by a host of ribosome assembly factors. Although it is known that many of the proteins involved in this process have RNA binding activity, the full repertoire of proteins that interact with the precursor ribosomal RNA is currently unknown. To gain a greater understanding of the extent to which RNA-protein interactions have the potential to control ribosome biogenesis, we used RNA affinity isolation coupled with proteomics to measure the changes in RNA-protein interactions that occur when rRNA transcription is blocked. Our analysis identified 211 out of 457 nuclear RNA binding proteins with a >3-fold decrease in RNA-protein interaction after inhibition of RNA polymerase I (RNAPI). We have designated these 211 RNA binding proteins as the RNAPI RNA interactome. As expected, the RNAPI RNA interactome is highly enriched for nucleolar proteins and proteins associated with ribosome biogenesis. Selected proteins from the interactome were shown to be nucleolar in location and to have RNA binding activity that was dependent on RNAPI activity. Furthermore, our data show that two proteins, which are required for rRNA maturation, AATF and NGDN, and which form part of the RNA interactome, both lack canonical RNA binding domains and yet are novel pre-rRNA binding proteins.

Indexed as

Protein BindingBenzothiazolesBinding, CompetitiveCell LineCell Line, TumorDactinomycinHumansNaphthyridinesNuclear ProteinsProteomicsRibosomal ProteinsRNA-Binding ProteinsRNA Polymerase IRNA PrecursorsRNA, RibosomalTranscription, GeneticBenzothiazolesCX 5461DactinomycinNaphthyridinesNuclear ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA Polymerase IRNA PrecursorsRNA, Ribosomal

Identifiers

PMID30169671
PMCPMC6237751
OpenAlexW2889500497

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.