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Posttranslational covalent modification of proteins.

R Uy, F Wold

    Science (New York, N.Y.)
    |December 2, 1977
    PubMed
    Summary
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    Posttranslational modification significantly expands the 20 genetic amino acids to about 140 derivatives in proteins. Further research is needed to understand the mechanisms and biological roles of these essential protein modifications.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Proteomics

    Background:

    • The genetic code specifies 20 standard amino acids for protein synthesis.
    • Proteins undergo substantial posttranslational modifications, creating numerous amino acid derivatives.
    • Approximately 140 amino acid derivatives have been identified in proteins across various organisms.

    Purpose of the Study:

    • To highlight the significant extent of posttranslational modification in proteins.
    • To identify key unanswered questions regarding the mechanisms and functions of these modifications.
    • To emphasize the need for further research in this area.

    Main Methods:

    • Literature review and analysis of existing data on protein constituents.
    • Identification and cataloging of known amino acid derivatives in proteins.

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  • Conceptual framework for future research directions.

    • Main Results:

    • Demonstrated that posttranslational modifications substantially increase the diversity of amino acid residues in proteins.
    • Identified around 140 distinct amino acid derivatives beyond the 20 standard ones.
    • Highlighted critical knowledge gaps concerning the timing, location, specificity, and biological facilitation of these modifications.

    Conclusions:

    • Posttranslational modifications represent a vast and underexplored area of protein diversity.
    • Understanding these modifications is crucial for advancing biochemistry and cell biology.
    • Further investigation into the 'how,' 'when,' 'where,' and 'why' of protein derivatization is warranted.