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The elongation factor 1 from wheat germ: structural and functional properties

J Pulikowska, T Twardowski

    Acta Biochimica Polonica
    |January 1, 1982
    PubMed
    Summary

    Wheat germ elongation factor 1 (EF1A) is crucial for protein synthesis, forming a ternary complex and binding aminoacyl-tRNA to ribosomes. EF1C appears to be a structural subunit, while EF1A possesses the full biological activity.

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    Area of Science:

    • Molecular Biology
    • Protein Synthesis
    • Biochemistry

    Background:

    • Elongation factor 1 (EF1) plays a vital role in protein synthesis by facilitating the delivery of aminoacyl-tRNA to the ribosome.
    • Wheat germ is a common source for isolating and studying plant-based protein synthesis machinery.

    Purpose of the Study:

    • To isolate and characterize the different forms of elongation factor 1 (EF1) from wheat germ.
    • To determine the specific roles and activities of each isolated EF1 form in protein synthesis.

    Main Methods:

    • Isolation of EF1 forms using sequential chromatography (DEAE-Sephadex A-50, hydroxylapatite, Sephadex G-200).
    • Determination of molecular masses for each isolated form.
    • Assay of ternary complex formation (GTP-EF1-AA-tRNA).

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  • Measurement of Phe-tRNA binding to poly-U programmed ribosomes.
  • Amino acid analysis and N-terminal amino acid determination.

    • Main Results:

    • Three forms of EF1 (EF1A, EF1B, EF1C) were isolated with high purity (approx. 90%).
    • Molecular masses were determined as approximately 61,000 (EF1A), 48,000 (EF1B), and 12,500 (EF1C).
    • EF1A was the sole form capable of forming the ternary complex and exhibited the highest activity in binding Phe-tRNA to ribosomes.

    Conclusions:

    • EF1A is the functionally active component of wheat germ elongation factor 1, essential for aminoacyl-tRNA binding.
    • EF1C is proposed to be a basic structural subunit of EF1, lacking full biological activity on its own.
    • The distinct forms of EF1 likely represent different functional or structural states involved in the complex process of protein elongation.