Evidence map›Paper›PMID 19033360›Full record

ArticleNucleic acids research2009

Structure of the yeast Pml1 splicing factor and its integration into the RES complex.

Mark A Brooks, Andrzej Dziembowski, Sophie Quevillon-Cheruel, Véronique Henriot, Céline Faux, Herman van Tilbeurgh, Bertrand Séraphin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

28 citing papers in PubMed, 53 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.

Mark A BrooksIBBMC-CNRS UMR8619, IFR 115, Université Paris-Sud, Orsay, France.
Andrzej Dziembowski
Sophie Quevillon-Cheruel
Véronique Henriot
Céline Faux
Herman van Tilbeurgh
Bertrand Séraphin
Sorbonne Université · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RES complex was previously identified in yeast as a splicing factor affecting nuclear pre-mRNA retention. This complex was shown to contain three subunits, namely Snu17, Bud13 and Pml1, but its mode of action remains ill-defined. To obtain insights into its function, we have performed a structural investigation of this factor. Production of a short N-terminal truncation of residues that are apparently disordered allowed us to determine the X-ray crystallographic structure of Pml1. This demonstrated that it consists mainly of a FHA domain, a fold which has been shown to mediate interactions with phosphothreonine-containing peptides. Using a new sensitive assay based on alternative splice-site choice, we show, however, that mutation of the putative phosphothreonine-binding pocket of Pml1 does not affect pre-mRNA splicing. We have also investigated how Pml1 integrates into the RES complex. Production of recombinant complexes, combined with serial truncation and mutagenesis of their subunits, indicated that Pml1 binds to Snu17, which itself contacts Bud13. This analysis allowed us to demarcate the binding sites involved in the formation of this assembly. We propose a model of the organization of the RES complex based on these results, and discuss the functional consequences of this architecture.

Indexed as

RNA SplicingAmino Acid SequenceCarrier ProteinsConserved SequenceCrystallography, X-RayModels, MolecularMolecular Sequence DataPhosphothreonineProtein Interaction Domains and MotifsProtein Structure, TertiaryProtein SubunitsRibonucleoprotein, U2 Small NuclearRNA Splice SitesSaccharomyces cerevisiae ProteinsSulfatesBud13 protein, S cerevisiaeCarrier ProteinsIST3 protein, S cerevisiaePhosphothreoninePml1 protein, S cerevisiaeProtein SubunitsRibonucleoprotein, U2 Small NuclearRNA Splice SitesSaccharomyces cerevisiae ProteinsSulfates

Identifiers

PMID19033360
PMCPMC2615620
OpenAlexW2033674796

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.