Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structuring of the 3' splice site by U2AF65.

Oliver A Kent1, Ayube Reayi, Louise Foong

  • 1Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.

The Journal of Biological Chemistry
|September 25, 2003
PubMed
Summary

The U2AF65 protein bends precursor mRNA (pre-mRNA) to facilitate spliceosome assembly. This interaction is crucial for recognizing the 3' splice site in mammalian introns, organizing RNA structures for splicing.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Selectively targeting inosine monophosphate dehydrogenase-2 impairs brain metastatic potential while preserving immune cell function.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Design of a peripherally biased NPSR1 antagonist for neuropeptide S induced inflammation.

Bioorganic & medicinal chemistry letters·2025
Same author

Interactome of FMRP-N-tat therapeutic unveils key interactions for cellular function in Fragile X neurons.

The Journal of biological chemistry·2025
Same author

Disruption of Plexin-A1 signaling by FTX-101: mode of action and effect on oligodendrocyte biology.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2025
Same author

Dynamic Coupling of MAPK Signaling to the Guanine Nucleotide Exchange Factor GEF-H1.

OncoTargets and therapy·2025
Same author

Spliceosome assembly and regulation: insights from analysis of highly reduced spliceosomes.

RNA (New York, N.Y.)·2023

Area of Science:

  • Molecular Biology
  • RNA Splicing
  • Protein-RNA Interactions

Background:

  • Spliceosome assembly requires U2AF binding to precursor mRNA (pre-mRNA) at the 3' splice site.
  • The orientation of U2AF65 domains and their role in the commitment complex are poorly understood, leading to conflicting models.

Purpose of the Study:

  • To investigate the structural role of U2AF65 domains in pre-mRNA recognition and commitment complex formation.
  • To resolve contradictory models regarding U2AF65's function in splicing.

Main Methods:

  • Utilized U2AF deletion mutants modified with an iron-EDTA hydroxyl radical probe.
  • Analyzed high-resolution X-ray structures of protein-RNA complexes.
  • Examined U2AF65 interaction with a 3' splice site RNA mimic.

Related Experiment Videos

Main Results:

  • Demonstrated that U2AF65 bends the pre-mRNA.
  • Showed that this bending juxtaposes key RNA functionalities.
  • Provided evidence for U2AF65's role in organizing structures for spliceosome assembly.

Conclusions:

  • Proposed a model where U2AF65-mediated pre-mRNA bending is essential for spliceosome commitment.
  • This structural organization facilitates subsequent steps in the splicing pathway.