Evidence map›Paper›PMID 22535589›Full record

ArticleRNA (New York, N.Y.)2012

Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS.

Thomas Ohrt, Mira Prior, Julia Dannenberg, Peter Odenwälder, Olexandr Dybkov, Nicolas Rasche, Jana Schmitzová, Ingo Gregor, Patrizia Fabrizio, Jörg Enderlein and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

61 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The structure of Prp2 bound to RNA and ADP-BeFActa crystallographica. Section D, Structural biology · 2021
    Article
  11. Article
  12. Article
  13. Structural Insights into Nuclear pre-mRNA Splicing in Higher Eukaryotes.Cold Spring Harbor perspectives in biology · 2019
    Review
  14. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    Review
  15. A U2-snRNP-independent role of SF3b in promoting mRNA export.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Review
  17. Article
  18. Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018
    Article
  19. Article
  20. Article

1 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

11 authors at 2 institutions in 1 country.

Thomas OhrtMax Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
Mira Prior
Julia Dannenberg
Peter Odenwälder
Olexandr Dybkov
Nicolas Rasche
Jana Schmitzová
Ingo Gregor
Patrizia Fabrizio
Jörg Enderlein
Reinhard Lührmann
Max Planck Institute for Biophysical Chemistry · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The compositional and conformational changes during catalytic activation of the spliceosome promoted by the DEAH box ATPase Prp2 are only poorly understood. Here, we show by dual-color fluorescence cross-correlation spectroscopy (dcFCCS) that the binding affinity of several proteins is significantly changed during the Prp2-mediated transition of precatalytic B(act) spliceosomes to catalytically activated B* spliceosomes from Saccharomyces cerevisiae. During this step, several proteins, including the zinc-finger protein Cwc24, are quantitatively displaced from the B* complex. Consistent with this, we show that Cwc24 is required for step 1 but not for catalysis per se. The U2-associated SF3a and SF3b proteins Prp11 and Cus1 remain bound to the B* spliceosome under near-physiological conditions, but their binding is reduced at high salt. Conversely, high-affinity binding sites are created for Yju2 and Cwc25 during catalytic activation, consistent with their requirement for step 1 catalysis. Our results suggest high cooperativity of multiple Prp2-mediated structural rearrangements at the spliceosome's catalytic core. Moreover, dcFCCS represents a powerful tool ideally suited to study quantitatively spliceosomal protein dynamics in equilibrium.

Indexed as

Catalytic DomainDEAD-box RNA HelicasesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectrometry, FluorescenceSpliceosomesDEAD-box RNA HelicasesPRP2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22535589
PMCPMC3358646
OpenAlexW2096352855

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.