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Related Experiment Videos

Sequential folding of a bifunctional allosteric protein.

J R Garel, A Dautry-Varsat

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1980
    PubMed
    Summary

    Aspartokinase I-homoserine dehydrogenase I refolds through sequential steps, regaining kinase and dehydrogenase activities. This process involves intermediate species with partial functions, ultimately forming a tetrameric enzyme sensitive to threonine.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Folding

    Background:

    • Aspartokinase I-homoserine dehydrogenase I is a bifunctional, allosteric enzyme.
    • Understanding its folding is crucial for enzyme function and stability.

    Purpose of the Study:

    • To investigate the renaturation process of aspartokinase I-homoserine dehydrogenase I.
    • To identify the sequential steps and intermediates involved in enzyme folding.

    Main Methods:

    • Monitoring the reappearance of kinase and dehydrogenase activities.
    • Assessing allosteric inhibition by threonine during refolding.
    • Analyzing the kinetics of folding to detect intermediate species.

    Main Results:

    • Refolding occurs in three successive steps: monomer formation, dimer formation, and tetramer formation.

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  • Intermediate species exhibit partial enzymatic activities and allosteric inhibition.
  • Kinase and dehydrogenase activities appear to fold somewhat independently.

    • Conclusions:

    • The folding of aspartokinase I-homoserine dehydrogenase I is a sequential process.
    • Functional properties are regained progressively as the protein structure becomes more complex.
    • The enzyme's distinct functional domains fold independently during renaturation.