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Related Experiment Videos

Multiple forms of elongation factor 1 from calf brain.

H M Moon, B Redfield, S Millard

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1973
    PubMed
    Summary

    Heavy and light forms of elongation factor 1 (EF-1) were purified from calf brain. The heavy EF-1 form, a complex of the light form, contains cholesterol and shows less efficient GTP and aminoacyl-tRNA binding.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cellular Biology

    Background:

    • Elongation factor 1 (EF-1) plays a crucial role in protein synthesis.
    • EF-1 exists in different molecular forms, influencing its function.
    • Understanding EF-1 heterogeneity is key to elucidating protein translation regulation.

    Purpose of the Study:

    • To characterize the heavy (EF-1(H)) and light (EF-1(L)) forms of elongation factor 1 from calf brain.
    • To investigate the composition and functional differences between EF-1(H) and EF-1(L).

    Main Methods:

    • Partial purification of EF-1 heavy and light forms from calf brain.
    • Molecular weight determination using biochemical assays.
    • Analysis of EF-1 composition for cholesterol content.

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  • Assays for aminoacyl-tRNA binding to ribosomes in the presence of GTP.

    • Main Results:

    • EF-1(H) (2.5 x 10(5) to >1 x 10(6) MW) appears to be a complex of EF-1(L) (50,000–60,000 MW).
    • EF-1(H) contains significant amounts of free and esterified cholesterol, unlike EF-1(L).
    • Both forms are active in aminoacyl-tRNA binding, but EF-1(L) reacts more efficiently with GTP and aminoacyl-tRNA.

    Conclusions:

    • Calf brain EF-1 exists in distinct heavy and light forms with differing properties.
    • Cholesterol content in EF-1(H) may influence its complex formation or function.
    • EF-1(L) exhibits higher catalytic efficiency in ribosome-mediated aminoacyl-tRNA binding compared to EF-1(H).