Evidence map›Paper›PMID 29054886›Full record

ArticleRNA (New York, N.Y.)2018

The SSU processome interactome in

Nicholas G Vincent, J Michael Charette, Susan J Baserga

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The dual nature of the nucleolus.Genes & development · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  14. Article
  15. 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

3 authors.

Nicholas G Vincent *Department of Microbiology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
J Michael Charette *Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Susan J BasergaDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA susan.baserga@yale.edu.

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Key factors in human ribosome biogenesisR01GM115710 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 2015 to 2018
$1.6M
RESEARCH TRAINING: RADIATION THERAPY, BIOLOGY, PHYSICST32CA009259 · NCI · YALE UNIVERSITY · PI GLAZER, PETER M · 1985 to 2009
$1.4M
NCI NIH HHS T32 CA009259NIGMS NIH HHS R01 GM115710NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Ribosome assembly is an evolutionarily conserved and energy intensive process required for cellular growth, proliferation, and maintenance. In yeast, assembly of the small ribosomal subunit (SSU) requires approximately 75 assembly factors that act in coordination to form the SSU processome, a 6 MDa ribonucleoprotein complex. The SSU processome is required for processing, modifying, and folding the preribosomal RNA (rRNA) to prepare it for incorporation into the mature SSU. Although the protein composition of the SSU processome has been known for some time, the interaction network of the proteins required for its assembly has remained poorly defined. Here, we have used a semi-high-throughput yeast two-hybrid (Y2H) assay and coimmunoprecipitation validation method to produce a high-confidence interactome of SSU processome assembly factors (SPAFs), providing essential insight into SSU assembly and ribosome biogenesis. Further, we used glycerol density-gradient sedimentation to reveal the presence of protein subcomplexes that have not previously been observed. Our work not only provides essential insight into SSU assembly and ribosome biogenesis, but also serves as an important resource for future investigations into how defects in biogenesis and assembly cause congenital disorders of ribosomes known as ribosomopathies.

Indexed as

Multiprotein ComplexesProtein Interaction MapsRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesMultiprotein ComplexesRibosomal ProteinsSaccharomyces cerevisiae Proteinsglycerol-gradient sedimentationinteractomeprotein–protein interaction (PPI)ribosome biogenesissmall subunit (SSU) processomesubcomplexes

Identifiers

PMID29054886
PMCPMC5733573

What OpenQuestion holds

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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.