Evidence map›Paper›PMID 25587180›Full record

ArticleRNA (New York, N.Y.)2015

Structural basis for recognition of intron branchpoint RNA by yeast Msl5 and selective effects of interfacial mutations on splicing of yeast pre-mRNAs.

Agata Jacewicz, Lidia Chico, Paul Smith, Beate Schwer, Stewart Shuman

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 31 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 3 institutions in 1 country.

Agata JacewiczMolecular Biology Program, Sloan-Kettering Institute, New York, New York 10065, USA.
Lidia ChicoMolecular Biology Program, Sloan-Kettering Institute, New York, New York 10065, USA Department of Microbiology and Immunology, Weill Cornell Medical College, New York, New York 10065, USA.
Paul SmithDepartment of Chemistry, Fordham University, Bronx, New York 10458, USA.
Beate SchwerDepartment of Microbiology and Immunology, Weill Cornell Medical College, New York, New York 10065, USA bschwer@med.cornell.edu s-shuman@ski.mskcc.org.
Stewart ShumanMolecular Biology Program, Sloan-Kettering Institute, New York, New York 10065, USA bschwer@med.cornell.edu s-shuman@ski.mskcc.org.
Cornell University · USFordham University · USKettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
mRNA Capping EnzymesR01GM052470 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SCHWER, BEATE, SHUMAN, STEWART H · 1995 to 2019
$9.9M
STRUCTURE/FUNCTION ANALYSIS OF SPLICEOSOMAL ATPASESR01GM050288 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI SCHWER, BEATE · 1994 to 2011
$3.9M
RNA caps and meiotic pre-mRNA splicingR01GM102961 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI SCHWER, BEATE · 2013 to 2016
$1.3M
NCI NIH HHS P30 CA008748NIGMS NIH HHS GM50288NIGMS NIH HHS GM52470NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM050288NIGMS NIH HHS R01 GM052470NIGMS NIH HHS R01 GM102961
6 · The paper itself

Abstract

Saccharomyces cerevisiae Msl5 orchestrates spliceosome assembly by binding the intron branchpoint sequence 5'-UACUAAC and, with its heterodimer partner protein Mud2, establishing cross intron-bridging interactions with the U1 snRNP at the 5' splice site. Here we define the central Msl5 KH-QUA2 domain as sufficient for branchpoint RNA recognition. The 1.8 Å crystal structure of Msl5-(KH-QUA2) bound to the branchpoint highlights an extensive network of direct and water-mediated protein-RNA and intra-RNA atomic contacts at the interface that illuminate how Msl5 recognizes each nucleobase of the UACUAAC element. The Msl5 structure rationalizes a large body of mutational data and inspires new functional studies herein, which reveal how perturbations of the Msl5·RNA interface impede the splicing of specific yeast pre-mRNAs. We also identify interfacial mutations in Msl5 that bypass the essentiality of Sub2, a DExD-box ATPase implicated in displacing Msl5 from the branchpoint in exchange for the U2 snRNP. These studies establish an atomic resolution framework for understanding splice site selection and early spliceosome dynamics.

Indexed as

Adenosine TriphosphatasesCrystallography, X-RayIntronsMutationProtein ConformationRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA PrecursorsRNA Splice SitesRNA SplicingRNA Splicing FactorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesAdenosine TriphosphatasesMSL5 protein, S cerevisiaeRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA-dependent ATPaseRNA PrecursorsRNA Splice SitesRNA Splicing FactorsSaccharomyces cerevisiae Proteinsbranchpoint binding proteinKH-QUA2 domainspliceosome assembly

Identifiers

PMID25587180
PMCPMC4338336
OpenAlexW2159664316

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.