GO:0030623 U5 snRNA binding: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0030623 U5 snRNA binding is a molecular function describing the selective interaction of a protein with the U5 small nuclear RNA (U5 snRNA).
• U5 snRNA binding is essential for spliceosome assembly and for maintaining the precision of pre-mRNA splicing, especially at exon boundaries.
• The U5 snRNP is a ribonucleoprotein particle in which proteins such as Prp8, Brr2 and Snu114 interact with U5 snRNA internal loop 1 during assembly.
• Prp8 positions U5 snRNA for 5-prime splice site recognition, linking U5 snRNA binding directly to splice-site selection.
• U5 snRNA interactions with exons help ensure splicing precision, and antisense oligonucleotide binding to U5 snRNP can expose the conserved loop of U5 snRNA.
• Defects in U5 snRNP components and splicing quality control have been linked to cancer immune evasion and to splicing-related disease mechanisms.
Description
GO:0030623 U5 snRNA binding is a molecular function defined as binding to a U5 small nuclear RNA (U5 snRNA). U5 snRNA is one of the small nuclear RNAs that form the core of the spliceosome, the machinery that removes introns from pre-mRNA. Proteins that bind U5 snRNA are therefore central to spliceosome assembly and to the fidelity of exon joining. Because U5 snRNA binding is a molecular interaction rather than a single enzymatic reaction, it is studied through structural, biochemical and genetic approaches that map RNA-protein contacts and test their consequences for splicing. The importance of U5 snRNA binding for researchers lies in its direct connection to splicing precision. U5 snRNA interacts with exon sequences at the splice sites, and this interaction helps align exons for ligation. The protein environment of the U5 snRNP, including Prp8, Brr2 and Snu114, assembles around U5 snRNA and regulates its accessibility and positioning. Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition, which means that U5 snRNA binding is not a passive interaction but part of the mechanism that selects splice sites. Studying U5 snRNA binding also matters because splicing quality control and U5 snRNP stability influence gene expression programs relevant to disease. RNA binding proteins that mediate a quality control mechanism of splicing have been identified, and a novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing. In cancer, splicing-related factors such as G3BP1 and SLU7 can jointly promote immune evasion by downregulating MHC-I via PI3K/Akt activation, illustrating how splicing machinery components connect to tumor biology. Together, these findings make U5 snRNA binding a focused entry point for understanding spliceosome function, splicing fidelity and disease-associated splicing defects.
U5 snRNA binding At A Glance
| GO ID | GO:0030623 |
|---|---|
| GO term | U5 snRNA binding |
| Ontology | molecular_function |
| Synonym | None listed |
| Definition | Binding to a U5 small nuclear RNA (U5 snRNA). |
| Major function | Selective interaction with U5 snRNA that supports U5 snRNP assembly, spliceosome function and splicing precision. |
| Representative proteins | Prp8, Brr2 and Snu114 interact with U5 snRNA internal loop 1 during U5 snRNP assembly. |
| Related particle | U5 small nuclear ribonucleoprotein particle (U5 snRNP). |
| Disease relevance | Splicing quality control and U5 snRNP stability are linked to splicing-related disease mechanisms and cancer biology. |
What Is GO:0030623?
In this article, GO:0030623 U5 snRNA binding is understood as the molecular function of selectively binding to a U5 small nuclear RNA (U5 snRNA). It is a molecular_function term in the Gene Ontology, meaning it describes what a gene product does at the molecular level rather than a whole pathway or cellular structure. The function is realized by proteins that contact U5 snRNA within the U5 small nuclear ribonucleoprotein particle (U5 snRNP) and that help assemble, stabilize or position U5 snRNA during spliceosome assembly. Because the definition is binding-based, the term does not by itself specify a catalytic activity; instead it captures the RNA-protein interaction that supports downstream events such as 5-prime splice site recognition and exon alignment.
Why Is U5 snRNA binding Important in Cell Biology?
U5 snRNA binding is important because it connects a specific RNA-protein interaction to the accuracy of pre-mRNA splicing. U5 snRNA interactions with exons ensure splicing precision, and the protein environment of the U5 snRNP assembles around U5 snRNA to regulate its function. Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition, so U5 snRNA binding contributes directly to splice-site selection. In addition, U5 snRNP stability and splicing quality control mechanisms depend on RNA-binding activities, and defects in these processes have been connected to cancer immune evasion and other splicing-related pathologies. For researchers, this makes GO:0030623 a useful functional handle for dissecting spliceosome assembly, splicing fidelity and disease-associated splicing defects.
• U5 snRNA binding supports spliceosome assembly by anchoring U5 snRNA within the U5 snRNP.
• It contributes to splicing precision through U5 snRNA interactions with exon sequences.
• It is linked to 5-prime splice site recognition via Prp8 positioning of U5 snRNA.
• It is required for U5 snRNP stability, as shown for the RNA-binding activity of ECD.
• It participates in splicing quality control mechanisms mediated by RNA binding proteins.
• It is relevant to cancer biology, where splicing-related factors such as G3BP1 and SLU7 promote immune evasion.
• It provides a molecular target for studying minor spliceosome architecture, as revealed by the structure of the activated human minor spliceosome.
• It can be probed experimentally by antisense oligonucleotide binding to U5 snRNP, which induces conformational changes exposing the conserved loop of U5 snRNA.
• It is a molecular_function term, making it suitable for functional annotation and enrichment analyses of splicing-related gene sets.
• It connects RNA-protein interaction data to downstream phenotypes such as splicing fidelity and gene expression changes.
What Happens During U5 snRNA binding?
Recognition and initial contact with U5 snRNA
In simple terms: Proteins first find and grip the U5 snRNA molecule.
U5 snRNA binding begins when proteins recognize U5 snRNA within the assembling U5 snRNP. The U5 snRNA internal loop 1 acts as a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly, indicating that specific RNA structural elements are used for protein recruitment. Antisense oligonucleotide binding to U5 snRNP can induce a conformational change that exposes the conserved loop of U5 snRNA, showing that U5 snRNA accessibility is dynamic and can be modulated by RNA-targeting reagents. These observations support a model in which U5 snRNA binding is a regulated recognition step rather than a static association.
Assembly of the U5 snRNP protein environment
In simple terms: A set of proteins builds a stable particle around the U5 snRNA.
After initial contact, U5 snRNA binding contributes to the assembly of the U5 snRNP protein environment. The U5 snRNA internal loop 1 serves as a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly, which means that multiple proteins converge on the same RNA element. A novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing, further linking U5 snRNA-associated protein interactions to particle stability. The structure of the activated human minor spliceosome provides architectural context for how U5 snRNA and its protein partners are arranged in an active splicing machine.
Positioning of U5 snRNA for splice-site recognition
In simple terms: The bound U5 snRNA is placed so it can read the splice site.
A key outcome of U5 snRNA binding is the positioning of U5 snRNA for 5-prime splice site recognition. Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition, which connects the binding function to splice-site selection. U5 snRNA interactions with exons ensure splicing precision, indicating that the spatial arrangement of U5 snRNA relative to exon sequences is functionally important. Together, these findings show that U5 snRNA binding is part of the mechanism that aligns the spliceosome with correct splice sites.
Quality control and splicing fidelity
In simple terms: The cell checks that splicing is done correctly and discards bad intermediates.
U5 snRNA binding also operates within splicing quality control pathways. RNA binding proteins that mediate a quality control mechanism of splicing have been identified, suggesting that RNA-protein interactions in the spliceosome are monitored for correctness. Because U5 snRNA interactions with exons ensure splicing precision, perturbations in U5 snRNA binding would be expected to affect fidelity. The stability of the U5 snRNP, supported by RNA-binding activities such as that of ECD, is likely important for maintaining a pool of functional splicing complexes.
Conformational changes and regulation of U5 snRNA accessibility
In simple terms: The U5 snRNA can change shape, and this changes which proteins can bind it.
U5 snRNA binding is not a fixed state; conformational changes can alter which regions of U5 snRNA are available for protein or oligonucleotide interaction. Antisense oligonucleotide binding to U5 snRNP induces a conformational change that exposes the conserved loop of U5 snRNA, demonstrating that the RNA can switch between conformations. Such dynamic behavior is consistent with the idea that U5 snRNA internal loop 1 acts as a protein-binding platform whose accessibility may be regulated during assembly. These features make U5 snRNA binding a dynamic molecular function that can be probed experimentally.
Key Genes Involved in GO:0030623 U5 snRNA binding
The genes and proteins most directly associated with GO:0030623 U5 snRNA binding are components of the U5 snRNP and splicing machinery that contact U5 snRNA or regulate its stability and positioning.
| Gene | Major Role | Research Relevance |
|---|---|---|
| PRPF8 (Prp8) | Positions U5 snRNA for 5-prime splice site recognition | Central scaffold for studying U5 snRNA positioning and splice-site selection |
| SNRNP200 (Brr2) | Binds U5 snRNA internal loop 1 during U5 snRNP assembly | Model for RNA-protein contacts in U5 snRNP assembly |
| SNU114 (Snu114) | Binds U5 snRNA internal loop 1 during U5 snRNP assembly | Component of the U5 snRNA protein-binding platform |
| ECD | Novel RNA-binding activity contributes to U5 snRNP stability and pre-mRNA splicing | Links U5 snRNP stability to splicing function |
| G3BP1 | Jointly promotes immune evasion with SLU7 via PI3K/Akt activation | Connects splicing-related factors to cancer immune evasion |
| SLU7 | Jointly promotes immune evasion with G3BP1 via PI3K/Akt activation | Splicing factor implicated in MHC-I downregulation in cancer |
| U5 snRNA | Small nuclear RNA bound by U5 snRNP proteins | Core RNA entity for GO:0030623 binding assays |
| Minor spliceosome U5 snRNA components | Part of the activated human minor spliceosome architecture | Structural studies of U5 snRNA-containing spliceosomes |
| RNA binding proteins in splicing quality control | Mediate a quality control mechanism of splicing | Candidate regulators of splicing fidelity |
| Prp8-associated factors | Support U5 snRNA positioning and splice-site recognition | Genetic and biochemical dissection of U5 snRNA function |
| Brr2-associated assembly factors | Participate in U5 snRNP assembly around U5 snRNA | Assembly assays and interaction mapping |
| Snu114-associated assembly factors | Participate in U5 snRNP assembly around U5 snRNA | Assembly assays and interaction mapping |
| ECD-associated splicing complexes | Contribute to U5 snRNP stability | Stability assays and splicing reporter systems |
| Spliceosome quality control factors | Monitor splicing correctness | Reporter-based quality control assays |
| MHC-I regulatory splicing network | Downregulated via PI3K/Akt in bladder cancer | Cancer immunology and splicing crosstalk studies |
| Exon-interacting U5 snRNA partners | Ensure splicing precision through exon interactions | Precision splicing assays |
| U5 snRNP structural proteins | Form the protein environment of U5 snRNA | Structural and biochemical studies |
| Antisense oligonucleotide targets in U5 snRNP | Induce conformational changes exposing the conserved U5 snRNA loop | Oligonucleotide-based probing of U5 snRNA conformation |
How Is U5 snRNA binding Regulated?
U5 snRNA binding is regulated at the level of RNA accessibility and protein assembly. Antisense oligonucleotide binding to U5 snRNP induces a conformational change that exposes the conserved loop of U5 snRNA, indicating that the RNA can be toggled between conformations that differ in protein accessibility. The U5 snRNA internal loop 1 acts as a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly, so the availability of this platform influences which proteins can bind. In addition, a novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing, suggesting that stability factors can regulate the functional pool of U5 snRNP. Splicing quality control mechanisms mediated by RNA binding proteins provide a further layer of regulation that monitors splicing correctness. Together, these findings indicate that U5 snRNA binding is controlled by conformational changes, protein assembly and quality control pathways.
U5 snRNA binding and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| G3BP1 | Bladder cancer immune evasion via MHC-I downregulation | Knockout in bladder cancer cell lines followed by MHC-I and PI3K/Akt readouts |
| SLU7 | Bladder cancer immune evasion via MHC-I downregulation | Knockout or knockdown in bladder cancer cells with immune evasion assays |
| ECD | U5 snRNP stability and pre-mRNA splicing defects | Knockout or point-mutation models to assess U5 snRNP stability |
| PRPF8 (Prp8) | Splice-site recognition defects | Point-mutation knock-in to test U5 snRNA positioning |
| SNRNP200 (Brr2) | U5 snRNP assembly defects | Knockout or tagged knock-in to map U5 snRNA interactions |
U5 snRNA binding and cancer immune evasion
Splicing-related factors connected to the U5 snRNP environment have been implicated in cancer immune evasion. G3BP1 and SLU7 jointly promote immune evasion by downregulating MHC-I via PI3K/Akt activation in bladder cancer, showing that splicing-associated proteins can influence tumor immunology. Because U5 snRNA binding is part of the spliceosome machinery that determines splicing outcomes, perturbations in U5 snRNP components could contribute to altered splicing programs in cancer. This makes U5 snRNA binding-related genes candidate modifiers of immune recognition in tumors.
U5 snRNP stability and splicing-related disease mechanisms
The stability of the U5 snRNP is important for pre-mRNA splicing, and a novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing. When U5 snRNP stability is compromised, splicing fidelity may be affected, and splicing quality control mechanisms mediated by RNA binding proteins may be engaged. These mechanisms are relevant to splicing-related diseases in which spliceosome components are dysfunctional. Studying U5 snRNA binding provides a way to dissect how stability defects translate into splicing changes.
Splicing precision and disease-associated splice-site selection
U5 snRNA interactions with exons ensure splicing precision, and Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition. Errors in splice-site selection can produce aberrant transcripts, and the U5 snRNP is directly involved in this process. Consequently, disease-associated mutations or expression changes in U5 snRNP proteins could alter splice-site choice. Experimental models that perturb U5 snRNA binding can therefore be used to study disease-relevant splicing defects.
Minor spliceosome architecture and disease relevance
The structure of the activated human minor spliceosome provides architectural information about U5 snRNA-containing complexes. Minor spliceosome components are distinct from the major spliceosome, and their dysfunction has been associated with disease phenotypes in the literature. Understanding how U5 snRNA is bound and positioned in the minor spliceosome can inform studies of splicing-related disorders. This structural context complements biochemical studies of U5 snRNA binding.
From U5 snRNA binding-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of a candidate U5 snRNA-binding protein impair splicing? | CRISPR knockout cell model with splicing reporter |
| Does a specific residue in Prp8 affect U5 snRNA positioning? | Point-mutation knock-in cell model |
| Where does a U5 snRNP protein contact U5 snRNA? | Tagged knock-in for RNA-protein crosslinking and pulldown |
| Does overexpression of a splicing factor alter splicing fidelity? | Overexpression cell model with RNA-seq readout |
| Does a U5 snRNP stability factor affect particle abundance? | Knockout plus biochemical fractionation of U5 snRNP |
| Can oligonucleotides alter U5 snRNA conformation? | Antisense oligonucleotide treatment of cells followed by structural probing |
How to Study the U5 snRNA binding Process
| Method | What It Measures | Typical Application |
|---|---|---|
| RNA immunoprecipitation | Physical association between a protein and U5 snRNA | Testing candidate U5 snRNA-binding proteins |
| Antisense oligonucleotide probing | Conformational accessibility of U5 snRNA | Detecting exposure of the conserved U5 snRNA loop |
| Structural biology (cryo-EM) | Architecture of U5 snRNA-containing spliceosomes | Modeling U5 snRNA position in the minor spliceosome |
| Splicing reporter assays | Splicing precision and exon joining | Testing effects of U5 snRNA-binding perturbations |
| Quality control reporter assays | Activation of splicing quality control | Identifying RNA binding proteins that mediate quality control |
| U5 snRNP stability assays | Abundance and integrity of U5 snRNP | Evaluating ECD and other stability factors |
| MHC-I and PI3K/Akt readouts | Immune evasion and signaling activation | Cancer cell models with splicing factor perturbations |
| Splice-site recognition assays | 5-prime splice site usage | Testing Prp8-dependent U5 snRNA positioning |
RNA-protein interaction mapping
Mapping U5 snRNA binding requires methods that detect direct RNA-protein contacts. The U5 snRNA internal loop 1 was identified as a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly, which implies the use of RNA-protein interaction assays. Antisense oligonucleotide binding to U5 snRNP induces a conformational change that exposes the conserved loop of U5 snRNA, providing a probe for U5 snRNA accessibility. These approaches can be combined with structural data from the activated human minor spliceosome to build models of U5 snRNA binding.
Structural biology of U5 snRNA-containing complexes
Structural biology provides architectural information about how U5 snRNA is bound. The structure of the activated human minor spliceosome has been determined, offering a framework for understanding U5 snRNA-containing spliceosomes. Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition, and structural models help explain how this positioning is achieved. These structural studies complement biochemical mapping of U5 snRNA internal loop 1 interactions.
Splicing fidelity and quality control assays
Functional studies of U5 snRNA binding often measure splicing outcomes. U5 snRNA interactions with exons ensure splicing precision, so assays that detect exon joining accuracy are directly relevant. RNA binding proteins that mediate a quality control mechanism of splicing have been identified, and quality control reporters can be used to test whether U5 snRNA-binding perturbations activate these pathways. A novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing, providing a specific example where stability and splicing readouts are combined.
Cancer and immune phenotyping
Because splicing-related factors can influence tumor immunology, U5 snRNA binding-related genes can be studied in cancer models. G3BP1 and SLU7 jointly promote immune evasion by downregulating MHC-I via PI3K/Akt activation in bladder cancer, illustrating how splicing factors are connected to immune phenotypes. Experimental workflows can combine genetic perturbation with MHC-I measurement and PI3K/Akt pathway readouts. These approaches help determine whether U5 snRNA binding-related genes affect immune recognition.
How CRISPR Can Be Used to Study GO:0030623 U5 snRNA binding
Knockout
CRISPR knockout is used to remove a candidate U5 snRNA-binding protein and test the consequences for splicing. For example, knocking out factors such as ECD can reveal effects on U5 snRNP stability and pre-mRNA splicing. Knockout of splicing-related factors such as G3BP1 or SLU7 can be combined with MHC-I and PI3K/Akt readouts to study immune evasion. Knockout models are therefore a first-line approach for linking a gene to U5 snRNA binding-related phenotypes.
Point Mutation
Point-mutation knock-in allows precise testing of residues involved in U5 snRNA binding. Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition, so mutations in Prp8 can be introduced to dissect this function. Point mutations can also be used to disrupt specific RNA-contact surfaces identified in U5 snRNP assembly studies. This approach separates binding from other functions of the same protein.
Knock-in
Tagged knock-in enables detection and purification of U5 snRNA-binding complexes. Tagging proteins such as Brr2, Snu114 or Prp8 can facilitate mapping of their interactions with U5 snRNA internal loop 1. Knock-in of affinity tags also supports structural and biochemical studies of U5 snRNP assembly. These models help connect molecular interactions to cellular splicing outcomes.
Overexpression
Overexpression models test whether increased levels of a splicing factor alter splicing or immune phenotypes. Overexpression of splicing-related factors can be combined with RNA-seq and immune readouts to assess effects on splicing programs. Because U5 snRNA interactions with exons ensure splicing precision, overexpression of U5 snRNA-binding proteins may affect fidelity. Overexpression is therefore useful for gain-of-function studies of U5 snRNA binding-related genes.
How EDITGENE Supports U5 snRNA binding Research
Researchers studying U5 snRNA binding-related genes often need to determine whether a candidate gene is causally involved in spliceosome assembly, splicing fidelity or disease-associated phenotypes. Establishing causality typically requires precise genetic perturbation followed by functional readouts such as splicing reporters, RNA-protein interaction assays and immune or signaling measurements. EDITGENE provides the cell-model and screening tools needed to move from candidate gene lists to mechanistic conclusions about U5 snRNA binding and its downstream effects.
Contact EDITGENE today to design your custom CRISPR model for U5 snRNA binding research.
Frequently Asked Questions About U5 snRNA binding
What is GO:0030623 U5 snRNA binding?
GO:0030623 U5 snRNA binding is a molecular_function term defined as binding to a U5 small nuclear RNA (U5 snRNA). It describes the selective interaction between a protein and U5 snRNA within the spliceosome machinery.
What genes are involved in U5 snRNA binding?
Genes and proteins associated with U5 snRNA binding include PRPF8 (Prp8), SNRNP200 (Brr2), SNU114 (Snu114) and ECD, which interact with or stabilize U5 snRNA-containing complexes. Splicing-related factors such as G3BP1 and SLU7 have also been linked to splicing-dependent cancer phenotypes.
Why is U5 snRNA binding important for splicing?
U5 snRNA interactions with exons ensure splicing precision, and Prp8 positioning of U5 snRNA is linked to 5-prime splice site recognition. This makes U5 snRNA binding central to accurate exon joining.
Which proteins bind U5 snRNA internal loop 1?
The U5 snRNA internal loop 1 is a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly. These proteins converge on the same RNA element to build the U5 snRNP.
How is U5 snRNA binding studied experimentally?
It is studied using RNA-protein interaction assays, structural biology of U5 snRNA-containing spliceosomes, splicing reporters and quality control assays. Antisense oligonucleotide probing can also reveal conformational changes in U5 snRNA.
Can antisense oligonucleotides change U5 snRNA conformation?
Yes, antisense oligonucleotide binding to U5 snRNP induces a conformational change that exposes the conserved loop of U5 snRNA. This demonstrates that U5 snRNA accessibility can be modulated experimentally.
What is the role of Prp8 in U5 snRNA binding?
Prp8 positions U5 snRNA, and this positioning is linked to 5-prime splice site recognition. Prp8 also binds U5 snRNA internal loop 1 during U5 snRNP assembly.
How does U5 snRNP stability relate to splicing?
A novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing, indicating that stable U5 snRNP particles are required for normal splicing. Splicing quality control mechanisms further monitor splicing correctness.
Is U5 snRNA binding relevant to cancer?
Splicing-related factors such as G3BP1 and SLU7 jointly promote immune evasion by downregulating MHC-I via PI3K/Akt activation in bladder cancer. This connects splicing machinery components to cancer immune biology.
What experimental models are used to study U5 snRNA binding?
Common models include CRISPR knockout, point-mutation knock-in, tagged knock-in and overexpression cell models, combined with splicing reporters and RNA-protein interaction assays. Structural studies of the minor spliceosome provide complementary architectural information.
Conclusion
GO:0030623 U5 snRNA binding captures a focused molecular interaction that sits at the heart of spliceosome function. U5 snRNA is bound by proteins such as Prp8, Brr2 and Snu114 during U5 snRNP assembly, and its positioning is linked to 5-prime splice site recognition and splicing precision. Stability factors such as ECD and quality control mechanisms mediated by RNA binding proteins add further layers of regulation. For researchers, U5 snRNA binding provides a tractable entry point for dissecting splicing fidelity and its disease connections, including cancer immune evasion. Combining structural insights from U5 snRNA-containing spliceosomes with CRISPR-based perturbation models enables mechanistic studies of how this binding function shapes gene expression and disease phenotypes.
References
- 1. Zheng X et al.. 2024. G3BP1 and SLU7 Jointly Promote Immune Evasion by Downregulating MHC-I via PI3K/Akt Activation in Bladder Cancer.. Adv Sci (Weinh) 11(7):e2305922 PMID: 38084438
- 2. Bai R et al.. 2021. Structure of the activated human minor spliceosome.. Science 371(6535) PMID: 33509932
- 3. Artemyeva-Isman OV et al.. 2021. U5 snRNA Interactions With Exons Ensure Splicing Precision.. Front Genet 12:676971 PMID: 34276781
- 4. Nancollis V et al.. 2013. The U5 snRNA internal loop 1 is a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly.. J Cell Biochem 114(12):2770-84 PMID: 23857713
- 5. Ast G et al.. 1997. Antisense oligonucleotide binding to U5 snRNP induces a conformational change that exposes the conserved loop of U5 snRNA.. Nucleic Acids Res 25(17):3508-13 PMID: 9254712
- 6. Arafat M et al.. 2025. Identification of RNA binding proteins that mediate a quality control mechanism of splicing.. bioRxiv PMID: 40777298
- 7. Raza M et al.. 2026. A novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing.. Nucleic Acids Res 54(14) PMID: 42478379
- 8. MacRae AJ et al.. 2018. Prp8 positioning of U5 snRNA is linked to 5' splice site recognition.. RNA 24(6):769-777 PMID: 29487104
