ArticleJournal of molecular biology2011
RNA induces conformational changes in the SF1/U2AF65 splicing factor complex.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- The distinct roles of zinc finger CCHC-type (ZCCHC) superfamily proteins in the regulation of RNA metabolism.RNA biology · 2021Review
- SF1 Phosphorylation Enhances Specific Binding to U2AFBiophysical journal · 2016Article
- A Structure-free Method for Quantifying Conformational Flexibility in proteins.Scientific reports · 2016Article
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- Structure of phosphorylated SF1 bound to U2AF⁶⁵ in an essential splicing factor complex.Structure (London, England : 1993) · 2013Article
- Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition.Nucleic acids research · 2013Article
- The mysterious RAMP proteins and their roles in small RNA-based immunity.Protein science : a publication of the Protein Society · 2012Review
- Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.Journal of molecular biology · 2012Article
- Branch point identification and sequence requirements for intron splicing in Plasmodium falciparum.Eukaryotic cell · 2011Article
- Purification, crystallization and preliminary X-ray crystallographic analysis of a central domain of human splicing factor 1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spliceosomes assemble on pre-mRNA splice sites through a series of dynamic ribonucleoprotein complexes, yet the nature of the conformational changes remains unclear. Splicing factor 1 (SF1) and U2 auxiliary factor (U2AF(65)) cooperatively recognize the 3' splice site during the initial stages of pre-mRNA splicing. Here, we used small-angle X-ray scattering to compare the molecular dimensions and ab initio shape restorations of SF1 and U2AF(65) splicing factors, as well as the SF1/U2AF(65) complex in the absence and presence of AdML (adenovirus major late) splice site RNAs. The molecular dimensions of the SF1/U2AF(65)/RNA complex substantially contracted by 15 Å in the maximum dimension, relative to the SF1/U2AF(65) complex in the absence of RNA ligand. In contrast, no detectable changes were observed for the isolated SF1 and U2AF(65) splicing factors or their individual complexes with RNA, although slight differences in the shapes of their molecular envelopes were apparent. We propose that the conformational changes that are induced by assembly of the SF1/U2AF(65)/RNA complex serve to position the pre-mRNA splice site optimally for subsequent stages of splicing.
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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.