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Is protein turnover thermodynamically controlled?

G McLendon, E Radany

    The Journal of Biological Chemistry
    |September 25, 1978
    PubMed
    Summary

    Protein stability in vitro correlates with degradation rates in vivo for most intracellular proteins. This suggests protein conformation influences cellular protein turnover control.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Proteomics

    Background:

    • Cellular processes rely on precise protein turnover.
    • Understanding protein degradation mechanisms is crucial for cell biology.

    Purpose of the Study:

    • To investigate the relationship between in vitro thermal stability and in vivo turnover rates of intracellular proteins.
    • To explore the implications of this relationship for protein turnover control models.

    Main Methods:

    • Parametric correlation analysis was used.
    • Nine intracellular proteins were studied.
    • In vitro thermal stability and in vivo turnover rates were measured.

    Main Results:

    • A significant parametric correlation (p < 0.01) was observed between in vitro thermal stability and in vivo turnover rates for most proteins studied.
    • Glyceraldehyde-3-phosphate dehydrogenase showed an inverse correlation, being stable in vivo but not in vitro.

    Conclusions:

    • Intramolecular conformation equilibria may play a key role in controlling intracellular protein degradation rates.
    • The findings support a "thermodynamic" model for protein turnover.
    • Glyceraldehyde-3-phosphate dehydrogenase represents a notable exception, warranting further investigation.

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