Evidence map›Paper›PMID 23754852›Full record

ArticleNucleic acids research2013

Structure-function analysis of the 5' end of yeast U1 snRNA highlights genetic interactions with the Msl5*Mud2 branchpoint-binding complex and other spliceosome assembly factors.

Beate Schwer, Jonathan Chang, Stewart Shuman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 22 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

3 authors at 2 institutions in 1 country.

Beate SchwerMicrobiology and Immunology Department, Weill Cornell Medical College, New York, NY 10065, USA and Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Jonathan Chang
Stewart Shuman
Cornell University · USKettering University · US

Funding

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
NIGMS NIH HHS GM50288NIGMS NIH HHS GM52470NIGMS NIH HHS R01 GM050288NIGMS NIH HHS R01 GM052470
6 · The paper itself

Abstract

Yeast pre-mRNA splicing initiates via formation of a complex comprising U1 snRNP bound at the 5' splice site (5'SS) and the Msl5•Mud2 heterodimer engaged at the branchpoint (BP). Here, we present a mutational analysis of the U1 snRNA, which shows that although enlarging the 5' leader between the TMG cap and the (3)ACUUAC(8) motif that anneals to the 5'SS is tolerated, there are tight constraints on the downstream spacer between (3)ACUUAC(8) and helix 1 of the U1 fold. We exploit U1 alleles with 5' extensions, variations in the (3)ACUUAC(8) motif, downstream mutations and a longer helix 1 to discover new intra-snRNP synergies with U1 subunits Nam8 and Mud1 and the trimethylguanosine (TMG) cap. We describe novel mutations in U1 snRNA that bypass the essentiality of the DEAD-box protein Prp28. Structure-guided mutagenesis of Msl5 distinguished four essential amino acids that contact the BP sequence from nine other BP-binding residues that are inessential. We report new synthetic genetic interactions of the U1 snRNP with Msl5 and Mud2 and with the nuclear cap-binding subunit Cbc2. Our results fortify the idea that spliceosome assembly can occur via distinct genetically buffered microscopic pathways involving cross-intron-bridging interactions of the U1 snRNP•5'SS complex with the Mud2•Msl5•BP complex.

Indexed as

AllelesBase PairingBase SequenceBinding SitesDNA Transposable ElementsMultiprotein ComplexesMutationNuclear Cap-Binding Protein ComplexProtein Interaction MappingRibonucleoproteinsRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA, FungalRNA Splicing FactorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCBC2 protein, S cerevisiaeDNA Transposable ElementsMSL5 protein, S cerevisiaeMUD2 protein, S cerevisiaeMultiprotein ComplexesNuclear Cap-Binding Protein ComplexRibonucleoproteinsRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA, FungalRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSplicing Factor U2AFU1A protein

Identifiers

PMID23754852
PMCPMC3753624
OpenAlexW2016589391

What OpenQuestion holds

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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.