Evidence map›Paper›PMID 26673715›Full record

ArticleNucleic acids research2016

Structural requirements for protein-catalyzed annealing of U4 and U6 RNAs during di-snRNP assembly.

Allison L Didychuk, Eric J Montemayor, David A Brow, Samuel E Butcher

Abstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Identification of transient intermediates during spliceosome activation by single molecule fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Structure and conformational plasticity of the U6 small nuclear ribonucleoprotein core.Acta crystallographica. Section D, Structural biology · 2017
    Article
  19. Article
  20. Substrate-assisted mechanism of RNP disruption by the spliceosomal Brr2 RNA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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

4 authors.

Allison L DidychukDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.
Eric J MontemayorDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA.
David A BrowDepartment of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA dabrow@wisc.edu.
Samuel E ButcherDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA butcher@biochem.wisc.edu.

Funding

Biophysical investigations of RNA complexes essential for gene expressionR35GM118131 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Samuel E Butcher · 2016 to 2026
$5.1M
Structure and Function of U6 Spliceosomal RNAR01GM065166 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BROW, DAVID A, BUTCHER, SAMUEL E · 2002 to 2016
$3.5M
NIGMS NIH HHS GM065166NIGMS NIH HHS R01 GM065166NIGMS NIH HHS R35 GM118131
6 · The paper itself

Abstract

Base-pairing of U4 and U6 snRNAs during di-snRNP assembly requires large-scale remodeling of RNA structure that is chaperoned by the U6 snRNP protein Prp24. We investigated the mechanism of U4/U6 annealing in vitro using an assay that enables visualization of ribonucleoprotein complexes and faithfully recapitulates known in vivo determinants for the process. We find that annealing, but not U6 RNA binding, is highly dependent on the electropositive character of a 20 Å-wide groove on the surface of Prp24. During annealing, we observe the formation of a stable ternary complex between U4 and U6 RNAs and Prp24, indicating that displacement of Prp24 in vivo requires additional factors. Mutations that stabilize the U6 'telestem' helix increase annealing rates by up to 15-fold, suggesting that telestem formation is rate-limiting for U4/U6 pairing. The Lsm2-8 complex, which binds adjacent to the telestem at the 3' end of U6, provides a comparable rate enhancement. Collectively, these data identify domains of the U6 snRNP that are critical for one of the first steps in assembly of the megaDalton U4/U6.U5 tri-snRNP complex, and lead to a dynamic model for U4/U6 pairing that involves a striking degree of evolved cooperativity between protein and RNA.

Indexed as

Base SequenceBinding, CompetitiveKineticsModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA, FungalRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPrp24 protein, S cerevisiaeRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA, FungalRNA, Small NuclearSaccharomyces cerevisiae ProteinsU4 small nuclear RNAU6 small nuclear RNA

Identifiers

PMID26673715
PMCPMC4756825

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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.