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Related Experiment Videos

Proteolytic precursor processing in the biosynthesis of mitochondria.

P C Heinrich, W Northemann, E Schmelzer

    Acta Biologica Et Medica Germanica
    |January 1, 1981
    PubMed
    Summary

    Mitochondrial proteins, like rat liver cytochrome c oxidase subunits IV and V, are synthesized as larger precursors, not polyproteins. These precursors contain extra peptide sequences and are synthesized on various polyribosomes.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Mitochondrial proteins are synthesized in the cytoplasm as precursors.
    • Processing of these precursors involves proteolytic enzymes, but their nature is largely unknown.
    • The biosynthesis of rat liver cytochrome c oxidase is a key area of study.

    Purpose of the Study:

    • To investigate the synthesis of rat liver cytochrome c oxidase subunits.
    • To determine if these subunits are synthesized as a polyprotein or individual precursors.
    • To characterize the precursors and their site of synthesis.

    Main Methods:

    • Analysis of in vivo and in vitro synthesized precursors.
    • Isolation and size analysis of messenger RNAs for subunits IV and V.
    • Investigation of the site of synthesis using polyribosome fractionation.

    Main Results:

    • Rat liver cytochrome c oxidase subunits IV and V are synthesized as larger molecular weight precursors, not a polyprotein.
    • Precursors to subunits IV and V exhibit an additional peptide sequence of approximately 3000 daltons.
    • Messenger RNAs for subunits IV and V have estimated lengths of 990±80 and 830±70 nucleotides, respectively.
    • Cytochrome c oxidase subunits IV and V are synthesized on free and membrane-bound polyribosomes.

    Conclusions:

    • Cytoplasmic subunits of rat liver cytochrome c oxidase are synthesized as distinct, larger precursors.
    • The findings contradict previous reports suggesting a polyprotein precursor.
    • The synthesis of these subunits occurs on a range of cellular polyribosomes.

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