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Related Experiment Videos

Characterization of initiation factor eIF-3 from wheat germ.

J W Checkley, L Cooley, J M Ravel

    The Journal of Biological Chemistry
    |February 25, 1981
    PubMed
    Summary

    Researchers purified wheat germ eukaryotic initiation factor 3 (eIF-3), a crucial protein complex for translation. This purified eIF-3 enhances messenger RNA binding to ribosomal subunits, a key step in protein synthesis.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Plant Science

    Background:

    • Eukaryotic initiation factor 3 (eIF-3) is essential for protein synthesis initiation.
    • Understanding the composition and function of eIF-3 in plants is crucial for deciphering translational regulation.

    Purpose of the Study:

    • To isolate and characterize wheat germ eIF-3.
    • To investigate the role of wheat germ eIF-3 in translation initiation.

    Main Methods:

    • Isolation of eIF-3 using DEAE-cellulose and phosphocellulose chromatography.
    • Purity assessment via glycerol gradient centrifugation and non-denaturing polyacrylamide gel electrophoresis (PAGE).
    • Subunit composition analysis using sodium dodecyl sulfate (SDS)-PAGE.

    Main Results:

    • Highly purified wheat germ eIF-3 (≥85% pure) was obtained.
    • Wheat germ eIF-3 comprises 11 distinct polypeptides with molecular weights ranging from 25,000 to 120,000.
    • Purified eIF-3 did not significantly inhibit 40S and 60S ribosomal subunit association or eIF-2 ternary complex formation.
    • Wheat germ eIF-3 enhanced the binding of Met-tRNAf to 40S ribosomal subunits in the presence of eIF-2 and GTP.

    Conclusions:

    • Wheat germ eIF-3 is a multi-subunit complex with a defined polypeptide composition.
    • Wheat germ eIF-3 plays a role in facilitating the recruitment of initiator tRNA to the 40S ribosomal subunit, independent of its effect on subunit association.

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