ArticleThe Journal of biological chemistry2014
A novel protein-protein interaction in the RES (REtention and Splicing) complex.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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.
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.
Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- Two distinct binding modes provide the RNA-binding protein RbFox with extraordinary sequence specificity.Nature communications · 2023Article
- An Arabidopsis Retention and Splicing complex regulates root and embryo development through pre-mRNA splicing.Plant physiology · 2022Article
- Kernel machine SNP set analysis finds the association of BUD13, ZPR1, and APOA5 variants with metabolic syndrome in Tehran Cardio-metabolic Genetics Study.Scientific reports · 2021Article
- Chasing coevolutionary signals in intrinsically disordered proteins complexes.Scientific reports · 2020Article
- RES complex is associated with intron definition and required for zebrafish early embryogenesis.PLoS genetics · 2018Article
- Article
- Association of BUD13 polymorphisms with metabolic syndrome in Chinese population: a case-control study.Lipids in health and disease · 2017Article
- Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.RNA (New York, N.Y.) · 2016Review
- The molecular basis for ANE syndrome revealed by the large ribosomal subunit processome interactome.eLife · 2016Article
- Graph theory and stability analysis of protein complex interaction networks.IET systems biology · 2016Article
- Interactions between RNA-binding proteins and P32 homologues in trypanosomes and human cells.Current genetics · 2016Article
- Gbp2 interacts with THO/TREX through a novel type of RRM domain.Nucleic acids research · 2016Article
- Retention and splicing complex (RES) - the importance of cooperativity.RNA biology · 2016Article
- Structures of intermediates during RES complex assembly.Scientific reports · 2015Article
- Dynamic Contacts of U2, RES, Cwc25, Prp8 and Prp45 Proteins with the Pre-mRNA Branch-Site and 3' Splice Site during Catalytic Activation and Step 1 Catalysis in Yeast Spliceosomes.PLoS genetics · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The retention and splicing (RES) complex is a conserved spliceosome-associated module that was shown to enhance splicing of a subset of transcripts and promote the nuclear retention of unspliced pre-mRNAs in yeast. The heterotrimeric RES complex is organized around the Snu17p protein that binds to both the Bud13p and Pml1p subunits. Snu17p exhibits an RRM domain that resembles a U2AF homology motif (UHM) and Bud13p harbors a Trp residue reminiscent of an UHM-ligand motif (ULM). It has therefore been proposed that the interaction between Snu17p and Bud13p resembles canonical UHM-ULM complexes. Here, we have used biochemical and NMR structural analysis to characterize the structure of the yeast Snu17p-Bud13p complex. Unlike known UHMs that sequester the Trp residue of the ULM ligand in a hydrophobic pocket, Snu17p and Bud13p utilize a large interaction surface formed around the two helices of the Snu17p domain. In total 18 residues of the Bud13p ligand wrap around the Snu17p helical surface in an U-turn-like arrangement. The invariant Trp(232) in Bud13p is located in the center of the turn, and contacts surface residues of Snu17p. The structural data are supported by mutational analysis and indicate that Snu17p provides an extended binding surface with Bud13p that is notably distinct from canonical UHM-ULM interactions. Our data highlight structural diversity in RRM-protein interactions, analogous to the one seen for nucleic acid interactions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.