Evidence map›Paper›PMID 18621711›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Evolution of an RNP assembly system: a minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster.

Matthias Kroiss, Jörg Schultz, Julia Wiesner, Ashwin Chari, Albert Sickmann, Utz Fischer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Microbiology (Reading, England) · 2026
    Review
  3. Article
  4. Article
  5. A unique mechanism of snRNP core assembly.Nature communications · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. DDX20: A Multifunctional Complex Protein.Molecules (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control.International journal of molecular sciences · 2020
    Review
  20. Article

3 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

6 authors.

Matthias KroissDepartment of Biochemistry, Theodor Boveri Institute, Biocenter, Am Hubland, 97074 Würzburg, Germany.
Jörg Schultz
Julia Wiesner
Ashwin Chari
Albert Sickmann
Utz Fischer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vertebrates, assembly of spliceosomal uridine-rich small nuclear ribonucleoproteins (UsnRNPs) is mediated by the SMN complex, a macromolecular entity composed of the proteins SMN and Gemins 2-8. Here we have studied the evolution of this machinery using complete genome assemblies of multiple model organisms. The SMN complex has gained complexity in evolution by a blockwise addition of Gemins onto an ancestral core complex composed of SMN and Gemin2. In contrast to this overall evolutionary trend to more complexity in metazoans, orthologs of most Gemins are missing in dipterans. In accordance with these bioinformatic data a previously undescribed biochemical purification strategy elucidated that the dipteran Drosophila melanogaster contains an SMN complex of remarkable simplicity. Surprisingly, this minimal complex not only mediates the assembly reaction in a manner very similar to its vertebrate counterpart, but also prevents misassembly onto nontarget RNAs. Our data suggest that only a minority of Gemins are required for the assembly reaction per se, whereas others may serve additional functions in the context of UsnRNP biogenesis. The evolution of the SMN complex is an interesting example of how the simplification of a biochemical process contributes to genome compaction.

Indexed as

Evolution, MolecularAnimalsCell Cycle ProteinsCell LineCyclic AMP Response Element-Binding ProteinDrosophila melanogasterDrosophila ProteinsGenome, InsectHistone ChaperonesIntracellular Signaling Peptides and ProteinsModels, GeneticMultiprotein ComplexesNerve Tissue ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA SplicingCell Cycle ProteinsCyclic AMP Response Element-Binding ProteinDrosophila ProteinsHira protein, DrosophilaHistone ChaperonesIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesNerve Tissue ProteinsRibonucleoproteins, Small NuclearRig protein, DrosophilaRNA-Binding ProteinsSMN Complex ProteinsTranscription Factors

Identifiers

PMID18621711
PMCPMC2481332

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.