ArticleRNA (New York, N.Y.)2011
Structural model of the p14/SF3b155 · branch duplex complex.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Bioinformatics analysis across pan-cancer and experimental validation in hepatocellular carcinoma revealed the oncogenic role of SF3B6.Frontiers in pharmacology · 2025Article
- Structural basis of branch site recognition by the human spliceosome.Science (New York, N.Y.) · 2022Article
- Overlapping roles of spliceosomal components SF3B1 and PHF5A in rice splicing regulation.Communications biology · 2021Article
- Rewards of divergence in sequences, 3-D structures and dynamics of yeast and human spliceosome SF3b complexes.Current research in structural biology · 2021Article
- Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019Review
- Genome-wide profiling of prognosis-related alternative splicing signatures in sarcoma.Annals of translational medicine · 2019Article
- Cryptic splicing events in the iron transporter ABCB7 and other key target genes in SF3B1-mutant myelodysplastic syndromes.Leukemia · 2016Article
- Structural and mechanistic insights into human splicing factor SF3b complex derived using an integrated approach guided by the cryo-EM density maps.RNA biology · 2016Article
- Group II intron lariat: Structural insights into the spliceosome.RNA biology · 2015Review
- Graded requirement for the spliceosome in cell cycle progression.Cell cycle (Georgetown, Tex.) · 2015Article
- The significant other: splicing by the minor spliceosome.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Human p14 (SF3b14), a component of the spliceosomal U2 snRNP, interacts directly with the pre-mRNA branch adenosine within the context of the bulged duplex formed between the pre-mRNA branch region and U2 snRNA. This association occurs early in spliceosome assembly and persists within the fully assembled spliceosome. Analysis of the crystal structure of a complex containing p14 and a peptide derived from p14-associated SF3b155 combined with the results of cross-linking studies has suggested that the branch nucleotide interacts with a pocket on a non-canonical RNA binding surface formed by the complex. Here we report a structural model of the p14 · bulged duplex interaction based on a combination of X-ray crystallography of an adenine p14/SF3b155 peptide complex, biochemical comparison of a panel of disulfide cross-linked protein-RNA complexes, and small-angle X-ray scattering (SAXS). These studies reveal specific recognition of the branch adenosine within the p14 pocket and establish the orientation of the bulged duplex RNA bound on the protein surface. The intimate association of one surface of the bulged duplex with the p14/SF3b155 peptide complex described by this model buries the branch nucleotide at the interface and suggests that p14 · duplex interaction must be disrupted before the first step of splicing.
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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.