Evidence map›Paper›PMID 18971323›Full record

ArticleRNA (New York, N.Y.)2008

Structure of yeast U6 snRNPs: arrangement of Prp24p and the LSm complex as revealed by electron microscopy.

Ramazan Karaduman, Prakash Dube, Holger Stark, Patrizia Fabrizio, Berthold Kastner, Reinhard Lührmann

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2008. 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
2.1field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  2. Article
  3. The sole LSm complex inRNA (New York, N.Y.) · 2017
    Article
  4. Article
  5. Structural analyses of the pre-mRNA splicing machinery.Protein science : a publication of the Protein Society · 2013
    Review
  6. Review
  7. Article
  8. Article
  9. Spliceosome structure and function.Cold Spring Harbor perspectives in biology · 2011
    Review
  10. Review
  11. Ribonucleoprotein multimers and their functions.Critical reviews in biochemistry and molecular biology · 2010
    Review
  12. Article
  13. Article
  14. Article
  15. 3' processing of eukaryotic precursor tRNAs.Wiley interdisciplinary reviews. RNA
    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

6 authors at 2 institutions in 1 country.

Ramazan KaradumanDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
Prakash Dube
Holger Stark
Patrizia Fabrizio
Berthold Kastner
Reinhard Lührmann
Max Planck Institute for Biophysical Chemistry · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein components of the U6 snRNP (Prp24p and LSm2-8) are thought to act cooperatively in facilitating the annealing of U6 and U4 snRNAs during U4/U6 di-snRNP formation. To learn more about the spatial arrangement of these proteins in S. cerevisiae U6 snRNPs, we investigated the structure of this particle by electron microscopy. U6 snRNPs, purified by affinity chromatography and gradient centrifugation, and then immediately adsorbed to the carbon film support, revealed an open form in which the Prp24 protein and the ring formed by the LSm proteins were visible as two separate morphological domains, while particles stabilized by chemical cross-linking in solution under mild conditions before binding to the carbon film exhibited a compact form, with the two domains in close proximity to one another. In the open form, individual LSm proteins were located by a novel approach employing C-terminal genetic tagging of the LSm proteins with yECitrine. These studies show the Prp24 protein at defined distances from each subunit of the LSm ring, which in turn suggests that the LSm ring is positioned in a consistent manner on the U6 RNA. Furthermore, in agreement with the EM observations, UV cross-linking revealed U6 RNA in contact with the LSm2 protein at the interface between Prp24p and the LSm ring. Further, LSmp-Prp24p interactions may be restricted to the closed form, which appears to represent the solution structure of the U6 snRNP particle.

Indexed as

Base SequenceMolecular Sequence DataRibonucleoprotein, U4-U6 Small NuclearRNA, FungalRNA, Small NuclearSaccharomyces cerevisiaeRibonucleoprotein, U4-U6 Small NuclearRNA, FungalRNA, Small NuclearU6 small nuclear RNA

Identifiers

PMID18971323
PMCPMC2590955
OpenAlexW2167660105

What OpenQuestion holds

Textmetadata
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.