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 Concept Videos

Leaky Scanning02:28

Leaky Scanning

5.3K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.3K

You might also read

Related Articles

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

Sort by
Same author

Radiopaque markers in children with functional constipation: Potential role in diagnosis, therapy, and outcomes.

Journal of pediatric gastroenterology and nutrition·2026
Same author

Rule-based natural language processing to extract clinical trial and research study enrollment history from unstructured notes.

Health informatics journal·2026
Same author

Artificial intelligence-based incident analysis and learning system to enhance patient safety and improve treatment quality.

NPJ digital medicine·2026
Same author

Effectiveness of massed cognitive processing therapy for posttraumatic stress disorder: A retrospective analysis.

Journal of traumatic stress·2026
Same author

Misleading Results in Posttraumatic Stress Disorder Predictive Models Using Electronic Health Record Data: Algorithm Validation Study.

Journal of medical Internet research·2025
Same author

Dynamics and Regulation of mRNA Cap Recognition by Human eIF4F.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Nov 3, 2025

Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization
05:23

Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization

Published on: December 23, 2020

6.3K

Single-Molecule Dynamics of SARS-CoV-2 5' Cap Recognition by Human eIF4F.

Hea Jin Hong, Matthew G Guevara, Eric Lin

    Biorxiv : the Preprint Server for Biology
    |June 2, 2021
    PubMed
    Summary

    The study reveals how translation factor eIF4F subunits coordinate to bind viral RNA caps, impacting coronavirus replication. Understanding this dynamic interplay is key for developing new antiviral strategies against SARS-CoV-2.

    More Related Videos

    Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques
    08:07

    Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques

    Published on: January 12, 2024

    942
    Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
    08:47

    Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

    Published on: May 1, 2020

    3.2K

    Related Experiment Videos

    Last Updated: Nov 3, 2025

    Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization
    05:23

    Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization

    Published on: December 23, 2020

    6.3K
    Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques
    08:07

    Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques

    Published on: January 12, 2024

    942
    Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
    08:47

    Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

    Published on: May 1, 2020

    3.2K

    Area of Science:

    • Molecular Biology
    • Virology
    • Biochemistry

    Background:

    • Coronaviruses, including SARS-CoV-2, rely on the eIF4F translation factor complex to initiate viral RNA translation via cap recognition.
    • The precise coordination of eIF4F subunits (eIF4E, eIF4G, eIF4A) during translation initiation and their impact on cap-binding efficiency remain incompletely understood.
    • Modulating eIF4F function is a potential strategy for inhibiting coronavirus replication.

    Approach:

    • Utilized a single-molecule fluorescence assay to monitor the interaction between the eIF4E cap-binding protein and the SARS-CoV-2 5'-UTR.
    • Investigated the roles of individual eIF4F subunits (eIF4A, eIF4G) and the complete eIF4F complex in cap recognition.
    • Assessed the effect of rocaglamide, an eIF4A inhibitor, on viral translation and the influence of eIF4E phosphorylation on cap-binding.

    Key Points:

    • Free eIF4A enhances the accessibility of the RNA cap for eIF4E binding, while eIF4G alone does not significantly alter eIF4E-RNA interaction kinetics.
    • The formation of the complete eIF4F complex markedly changes eIF4E-cap interactions, indicating that coordinated eIF4E and eIF4A activities determine overall cap recognition efficiency.
    • The phosphomimetic mutant eIF4E(S209D) exhibits enhanced binding to the viral 5'-UTR compared to wild-type eIF4E, suggesting a role for phosphorylation in regulating cap recognition.

    Conclusions:

    • The study elucidates the dynamic interplay between eIF4F subunits and viral RNA during translation initiation.
    • Coordinated action of eIF4E and eIF4A is crucial for efficient cap recognition on the SARS-CoV-2 5'-UTR.
    • Findings provide insights into the mechanisms of viral translation and potential targets for antiviral drug development.