Evidence map›Paper›PMID 24014766›Full record

ArticleEukaryotic cell2013

Structural and functional characterization of the N terminus of Schizosaccharomyces pombe Cwf10.

S Brent Livesay, Scott E Collier, Danny A Bitton, Jürg Bähler, Melanie D Ohi

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 13 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

5 authors at 2 institutions in 2 countries.

S Brent LivesayDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Scott E Collier
Danny A Bitton
Jürg Bähler
Melanie D Ohi
Vanderbilt University Medical Center · USUniversity College London · GB

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
BIOCHEMICAL &CHEMICAL TRAINING FOR CANCER RESEARCHT32CA009582 · NCI · VANDERBILT UNIVERSITY · PI David K Cortez · 1987 to 2026
$8.8M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Multifaceted Approaches for Studying the Structure and Function of SpliceosomesDP2OD004483 · OD · VANDERBILT UNIVERSITY · PI OHI, MELANIE DIANE · 2008 to 2008
$2.3M
NCI NIH HHS P30 CA068485NCI NIH HHS P30 CA68485NCI NIH HHS T32 CA009582NIGMS NIH HHS T32 GM008320NIGMS NIH HHS T32 GM08320NIH HHS DP2 OD004483NIH HHS DP2OD004483Wellcome Trust 095598
6 · The paper itself

Abstract

The spliceosome is a dynamic macromolecular machine that catalyzes the removal of introns from pre-mRNA, yielding mature message. Schizosaccharomyces pombe Cwf10 (homolog of Saccharomyces cerevisiae Snu114 and human U5-116K), an integral member of the U5 snRNP, is a GTPase that has multiple roles within the splicing cycle. Cwf10/Snu114 family members are highly homologous to eukaryotic translation elongation factor EF2, and they contain a conserved N-terminal extension (NTE) to the EF2-like portion, predicted to be an intrinsically unfolded domain. Using S. pombe as a model system, we show that the NTE is not essential, but cells lacking this domain are defective in pre-mRNA splicing. Genetic interactions between cwf10-ΔNTE and other pre-mRNA splicing mutants are consistent with a role for the NTE in spliceosome activation and second-step catalysis. Characterization of Cwf10-NTE by various biophysical techniques shows that in solution the NTE contains regions of both structure and disorder. The first 23 highly conserved amino acids of the NTE are essential for its role in splicing but when overexpressed are not sufficient to restore pre-mRNA splicing to wild-type levels in cwf10-ΔNTE cells. When the entire NTE is overexpressed in the cwf10-ΔNTE background, it can complement the truncated Cwf10 protein in trans, and it immunoprecipitates a complex similar in composition to the late-stage U5.U2/U6 spliceosome. These data show that the structurally flexible NTE is capable of independently incorporating into the spliceosome and improving splicing function, possibly indicating a role for the NTE in stabilizing conformational rearrangements during a splice cycle.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding SitesGTP PhosphohydrolasesMolecular Sequence DataMutationProtein BindingProtein Structure, TertiaryRibonucleoprotein, U5 Small NuclearRNA SplicingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSpliceosomesCwf10 protein, S pombeGTP PhosphohydrolasesRibonucleoprotein, U5 Small NuclearSchizosaccharomyces pombe Proteins

Identifiers

PMID24014766
PMCPMC3837936
OpenAlexW2129073132

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.