Evidence map›Paper›PMID 24130456›Full record

ArticlePLoS biology2013

An RNA-binding complex involved in ribosome biogenesis contains a protein with homology to tRNA CCA-adding enzyme.

Jinzhong Lin, Jing Lu, Yingang Feng, Mengyi Sun, Keqiong Ye

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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  7. Article
  8. Article
  9. The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020
    Review
  10. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. The complete structure of the small-subunit processome.Nature structural & molecular biology · 2017
    Article
  19. Article
  20. Article
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

5 authors at 3 institutions in 1 country.

Jinzhong LinNational Institute of Biological Sciences, Beijing, China.
Jing Lu
Yingang Feng
Mengyi Sun
Keqiong Ye
National Institute of Biological Sciences, Beijing · CNChinese Academy of Medical Sciences & Peking Union Medical College · CNQingdao Institute of Bioenergy and Bioprocess Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A multitude of proteins and small nucleolar RNAs transiently associate with eukaryotic ribosomal RNAs to direct their modification and processing and the assembly of ribosomal proteins. Utp22 and Rrp7, two interacting proteins with no recognizable domain, are components of the 90S preribosome or the small subunit processome that conducts early processing of 18S rRNA. Here, we determine the cocrystal structure of Utp22 and Rrp7 complex at 1.97 Å resolution and the NMR structure of a C-terminal fragment of Rrp7, which is not visible in the crystal structure. The structure reveals that Utp22 surprisingly resembles a dimeric class I tRNA CCA-adding enzyme yet with degenerate active sites, raising an interesting evolutionary connection between tRNA and rRNA processing machineries. Rrp7 binds extensively to Utp22 using a deviant RNA recognition motif and an extended linker. Functional sites on the two proteins were identified by structure-based mutagenesis in yeast. We show that Rrp7 contains a flexible RNA-binding C-terminal tail that is essential for association with preribosomes. RNA-protein crosslinking shows that Rrp7 binds at the central domain of 18S rRNA and shares a neighborhood with two processing H/ACA snoRNAs snR30 and snR10. Depletion of snR30 prevents the stable assembly of Rrp7 into preribosomes. Our results provide insight into the evolutionary origin and functional context of Utp22 and Rrp7.

Indexed as

Structural Homology, ProteinAmino Acid SequenceBinding SitesCross-Linking ReagentsMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMultiprotein ComplexesNuclear ProteinsProtein BindingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRibosomal ProteinsRibosomesRNA-Binding ProteinsCross-Linking ReagentsMultiprotein ComplexesNuclear ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA NucleotidyltransferasesRRP7 protein, S cerevisiaeSaccharomyces cerevisiae ProteinstRNA nucleotidyltransferaseUtp22 protein, S cerevisiae

Identifiers

PMID24130456
PMCPMC3794860
OpenAlexW2029196741

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.