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

The regulation of eIF-2 function protein synthesis initiation

B Safer, R Jagus

    Biochimie
    |August 1, 1981
    PubMed
    Summary

    Protein synthesis regulation involves more than just phosphorylation. Eukaryotic initiation factor 2 (eIF-2) activity is complex, involving its catalytic recycling, not just binding.

    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

    Use of dried milk for immunoblotting.

    Methods in molecular biology (Clifton, N.J.)·2011
    Same author

    Real-time PCR-based assay for quantitative detection of Hematodinium sp. in the blue crab Callinectes sapidus.

    Diseases of aquatic organisms·2009
    Same author

    In vitro translation.

    Current protocols in cell biology·2008
    Same author

    Inactivation of Escherichia coli by a combination of nisin, pulsed electric fields, and water activity reduction by sodium chloride.

    Journal of food protection·2002
    Same author

    New ways of initiating translation in eukaryotes.

    Molecular and cellular biology·2001
    Same author

    Phosphorylation of eukaryotic initiation factor 4E (eIF4E) at Ser209 is not required for protein synthesis in vitro and in vivo.

    European journal of biochemistry·2001

    Area of Science:

    • Molecular Biology
    • Protein Synthesis
    • Gene Expression Regulation

    Background:

    • Eukaryotic initiation factor 2 (eIF-2) is crucial for protein synthesis initiation.
    • Its regulation is thought to involve phosphorylation/dephosphorylation and ancillary factors affecting methionyl-tRNAi binding.

    Purpose of the Study:

    • To investigate the complex mechanisms regulating eIF-2 activity during protein synthesis initiation.
    • To explore factors beyond direct binding modulation.

    Main Methods:

    • Analysis of eIF-2 phosphorylation state in hemin-deficient lysates.
    • Investigation of covalent modifications affecting eIF-2 utilization efficiency.

    Main Results:

    • Data suggests eIF-2 regulation is more complex than previously assumed.
    • Modulation of eIF-2 activity involves alterations in its catalytic recycling.

    Conclusions:

    • The regulation of eIF-2 activity extends beyond simple phosphorylation or binding interactions.
    • Catalytic recycling of eIF-2 is a key component in its complex regulatory network.

    Related Experiment Videos