Evidence map›Paper›PMID 8943336›Full record

ArticleMolecular and cellular biology1996

Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing.

S H Kim, R J Lin

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

80 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
  2. Article
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  6. Arresting Spliceosome Intermediates at Various Stages of the Splicing Pathway.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Article
  8. The structure of Prp2 bound to RNA and ADP-BeFActa crystallographica. Section D, Structural biology · 2021
    Article
  9. DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021
    Review
  10. Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018
    Article
  13. Article
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  15. Article
  16. Article
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20 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

2 authors at 1 institution in 1 country.

S H KimDepartment of Molecular Biology, Beckman Research Institute of the City of Hope, Duarte, California 91010-3000, USA.
R J Lin
City Of Hope National Medical Center · US

Funding

FUNCTIONAL SPLICEOSOMES AND EXTRINSIC SPLICING FACTORSR01GM040639 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIN, REN-JANG · 1988 to 2006
$2.0M
NIGMS NIH HHS GM40639
6 · The paper itself

Abstract

In addition to small nuclear RNAs and spliceosomal proteins, ATP hydrolysis is needed for nuclear pre-mRNA splicing. A number of RNA-dependent ATPases which are involved in several distinct ATP-dependent steps in splicing have been identified in Saccharomyces cerevisiae and mammals. These so-called DEAD/H ATPases contain conserved RNA helicase motifs, although RNA unwinding activity has not been demonstrated in purified proteins. Here we report the role of one such DEAH protein, PRP2 of S. cerevisiae, in spliceosome activation. PRP2 bound to a precatalytic spliceosome prior to the first step of splicing. By blocking the activity of a novel splicing factor(s), HP, which was involved in a post-PRP2 step, we found that PRP2 hydrolyzed ATP to cause a change in the spliceosome without the occurrence of splicing. The change was quite dramatic and could account for the previously reported differences between the precatalytic, pre-mRNA-containing spliceosome and the "active," intermediate-containing spliceosome. The post-PRP2-ATP spliceosome was further isolated and could carry out the subsequent reaction apparently in the absence of PRP2 and ATP. We hypothesize that PRP2 functions as a molecular motor, similar to some DExH ATPases in transcription, in the activation of the precatalytic spliceosome for the transesterification reaction.

Indexed as

Gene Expression Regulation, FungalRNA SplicingSaccharomyces cerevisiae ProteinsAnimalsDEAD-box RNA HelicasesFungal ProteinsMammalsRNA, FungalRNA PrecursorsSaccharomyces cerevisiaeDEAD-box RNA HelicasesFungal ProteinsPRP2 protein, S cerevisiaeRNA, FungalRNA PrecursorsSaccharomyces cerevisiae Proteins

Identifiers

PMID8943336
PMCPMC231684
OpenAlexW1924714349

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.