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Postribosomal complexes containing eukaryotic initiation factor eIF-2.

H Amesz, T Haubrich, H O Voorma

    Molecular Biology Reports
    |May 31, 1979
    PubMed
    Summary
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    Eukaryotic initiation factors (eIFs) were found in post-ribosomal subunits. A novel complexed factor, separate from eIF-2, was identified that significantly stimulates amino acid incorporation and counteracts the heme-regulated inhibitor.

    Area of Science:

    • Molecular Biology
    • Protein Biochemistry
    • Cellular Regulation

    Background:

    • Eukaryotic initiation factors (eIFs) are crucial for protein synthesis.
    • These factors are known to associate with ribosomal subunits.
    • Understanding the composition and function of eIFs is vital for cellular processes.

    Purpose of the Study:

    • To analyze the activities of eukaryotic initiation factors in post-ribosomal subunits.
    • To identify and characterize free and complexed forms of these factors.
    • To investigate a novel activity that stimulates amino acid incorporation.

    Main Methods:

    • Zonal centrifugation was employed to separate factor activities.
    • Sepharose-heparin affinity chromatography was used for further purification.

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  • Analysis of sedimentation values (Svedberg units) to determine factor states.

    • Main Results:

    • Eukaryotic initiation factors were identified in the post-ribosomal supernatant.
    • Factors were found to exist as free entities (4-7S) and complexed forms (16-20S).
    • A complexed fraction containing eIF-2 also harbored a potent stimulatory activity for amino acid incorporation, counteracting the heme-regulated inhibitor.

    Conclusions:

    • Eukaryotic initiation factors exist in distinct free and complexed states.
    • A novel protein complex, distinct from eIF-2, enhances protein synthesis initiation.
    • This newly identified activity plays a role in regulating translation and may counteract inhibitory mechanisms like the heme-regulated inhibitor.