Evidence map›Paper›PMID 27683217›Full record

ArticleNucleic acids research2017

Stoichiometries of U2AF35, U2AF65 and U2 snRNP reveal new early spliceosome assembly pathways.

Li Chen, Robert Weinmeister, Jana Kralovicova, Lucy P Eperon, Igor Vorechovsky, Andrew J Hudson, Ian C Eperon

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. 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
1.6field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Li ChenUniversity of Leicester, Leicester Institute for Structural and Chemical Biology and Department of Molecular and Cell Biology, Leicester LE1 9HN, UK.
Robert WeinmeisterUniversity of Leicester, Leicester Institute for Structural and Chemical Biology and Department of Molecular and Cell Biology, Leicester LE1 9HN, UK.
Jana KralovicovaUniversity of Southampton, Faculty of Medicine, Southampton SO16 6YD, UK.
Lucy P EperonUniversity of Leicester, Leicester Institute for Structural and Chemical Biology and Department of Molecular and Cell Biology, Leicester LE1 9HN, UK.
Igor VorechovskyUniversity of Southampton, Faculty of Medicine, Southampton SO16 6YD, UK.
Andrew J HudsonUniversity of Leicester, Leicester Institute for Structural and Chemical Biology and Department of Chemistry, Leicester LE1 7RH, UK.
Ian C EperonUniversity of Leicester, Leicester Institute for Structural and Chemical Biology and Department of Molecular and Cell Biology, Leicester LE1 9HN, UK.
University of Leicester · GBUniversity of Southampton · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The selection of 3΄ splice sites (3΄ss) is an essential early step in mammalian RNA splicing reactions, but the processes involved are unknown. We have used single molecule methods to test whether the major components implicated in selection, the proteins U2AF35 and U2AF65 and the U2 snRNP, are able to recognize alternative candidate sites or are restricted to one pre-specified site. In the presence of adenosine triphosphate (ATP), all three components bind in a 1:1 stoichiometry with a 3΄ss. Pre-mRNA molecules with two alternative 3΄ss can be bound concurrently by two molecules of U2AF or two U2 snRNPs, so none of the components are restricted. However, concurrent occupancy inhibits splicing. Stoichiometric binding requires conditions consistent with coalescence of the 5΄ and 3΄ sites in a complex (I, initial), but if this cannot form the components show unrestricted and stochastic association. In the absence of ATP, when complex E forms, U2 snRNP association is unrestricted. However, if protein dephosphorylation is prevented, an I-like complex forms with stoichiometric association of U2 snRNPs and the U2 snRNA is base-paired to the pre-mRNA. Complex I differs from complex A in that the formation of complex A is associated with the loss of U2AF65 and 35.

Indexed as

RNA SplicingAdenosine TriphosphateCell LineHumansIntronsModels, BiologicalMultiprotein ComplexesPhosphoric Monoester HydrolasesProtein BindingRibonucleoprotein, U1 Small NuclearRNA PrecursorsRNA Splice SitesSpliceosomesSplicing Factor U2AFSurvival of Motor Neuron 2 ProteinTropomyosinAdenosine TriphosphateMultiprotein ComplexesPhosphoric Monoester HydrolasesRibonucleoprotein, U1 Small NuclearRNA PrecursorsRNA Splice SitesSplicing Factor U2AFSurvival of Motor Neuron 2 ProteinTPM1 protein, humanTropomyosin

Identifiers

PMID27683217
PMCPMC5389562
OpenAlexW2524681724

What OpenQuestion holds

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LicenceCC BY
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.