Evidence map›Paper›PMID 28636603›Full record

ArticleNature2017

Trans-kingdom mimicry underlies ribosome customization by a poxvirus kinase.

Sujata Jha, Madeline G Rollins, Gabriele Fuchs, Dean J Procter, Elizabeth A Hall, Kira Cozzolino, Peter Sarnow, Jeffrey N Savas, Derek Walsh

Abstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 4% 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

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 94 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Specific nucleotide substitutions in the burst sequence enhanceApplied and environmental microbiology · 2025
    Article
  13. Review
  14. Specialized ribosomes: integrating new insights and current challenges.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  15. Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

9 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Sujata JhaDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Madeline G RollinsDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Gabriele FuchsThe RNA Institute, Department of Biological Sciences, University at Albany-SUNY, Albany, New York 12222, USA.
Dean J ProcterDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Elizabeth A HallDepartment of Neurology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Kira CozzolinoDepartment of Neurology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Peter SarnowDepartment of Microbiology &Immunology, Stanford University School of Medicine, Stanford, California 94305, USA.
Jeffrey N SavasDepartment of Neurology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Derek WalshDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Northwestern University · USStanford University · USUniversity at Albany, State University of New York · US

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
Poxvirus manipulation of the host cell protein synthesis machineryR01AI127456 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Peter Shen, Derek Walsh · 2017 to 2026
$4.4M
Modulation of internal ribosome entry by ribosomal protein RPS25R01AI099506 · NIAID · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D, SARNOW, PETER · 2014 to 2018
$2.9M
Proteome Biology of Noise Induced Hearing LossR00DC013805 · NIDCD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SAVAS, JEFFREY NICHOLAS · 2015 to 2017
$747k
Translational control of gene expression during poxvirus infectionR21AI105330 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WALSH, DEREK · 2014 to 2015
$428k
NIAID NIH HHS R01 AI099506NIAID NIH HHS R01 AI127456NIAID NIH HHS R21 AI105330NIDCD NIH HHS R00 DC013805NIGMS NIH HHS T32 GM008061
6 · The paper itself

Abstract

Ribosomes have the capacity to selectively control translation through changes in their composition that enable recognition of specific RNA elements. However, beyond differential subunit expression during development, evidence for regulated ribosome specification within individual cells has remained elusive. Here we report that a poxvirus kinase phosphorylates serine/threonine residues in the human small ribosomal subunit protein, receptor for activated C kinase (RACK1), that are not phosphorylated in uninfected cells or cells infected by other viruses. These modified residues cluster in an extended loop in RACK1, phosphorylation of which selects for translation of viral or reporter mRNAs with 5' untranslated regions that contain adenosine repeats, so-called polyA-leaders. Structural and phylogenetic analyses revealed that although RACK1 is highly conserved, this loop is variable and contains negatively charged amino acids in plants, in which these leaders act as translational enhancers. Phosphomimetics and inter-species chimaeras have shown that negative charge in the RACK1 loop dictates ribosome selectivity towards viral RNAs. By converting human RACK1 to a charged, plant-like state, poxviruses remodel host ribosomes so that adenosine repeats erroneously generated by slippage of the viral RNA polymerase confer a translational advantage. Our findings provide insight into ribosome customization through trans-kingdom mimicry and the mechanics of species-specific leader activity that underlie poxvirus polyA-leaders.

Indexed as

Biological MimicryProtein Biosynthesis5' Untranslated RegionsAdenosineAmino Acid SequenceDNA-Directed RNA PolymerasesHumansModels, MolecularNeoplasm ProteinsPhosphorylationPoly AReceptors for Activated C KinaseRibosomesRNA, ViralVaccinia virusViral Proteins5' Untranslated RegionsAdenosineDNA-Directed RNA PolymerasesNeoplasm ProteinsPoly ARACK1 protein, humanReceptors for Activated C KinaseRNA, ViralVB1R protein, Vaccinia virusViral Proteins

Identifiers

PMID28636603
PMCPMC5526112
OpenAlexW2718067945

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.