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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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Related Experiment Video

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Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays
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Published on: November 12, 2012

Degradation of missense mutant beta-galactosidase proteins in Escherichia coli K-12.

P L Bergquist, P Truman

    Molecular & General Genetics : MGG
    |August 4, 1978
    PubMed
    Summary

    Ten of 43 Escherchia coli lacZ gene mutations caused protein degradation in vivo. No clear link was found between degradation and mutation position, subunit changes, or protein half-life.

    Area of Science:

    • Molecular Biology
    • Genetics
    • Protein Biochemistry

    Background:

    • The lacZ gene in Escherchia coli encodes beta-galactosidase, a crucial enzyme for lactose metabolism.
    • Missense mutations can alter protein structure and function, potentially leading to degradation.
    • Understanding protein stability and degradation pathways is vital in molecular biology.

    Purpose of the Study:

    • To investigate the in vivo degradation of mutant beta-galactosidase proteins.
    • To determine if there are correlations between protein degradation and other mutation-associated properties.

    Main Methods:

    • Analysis of 43 missense mutations in the Escherchia coli lacZ gene.
    • Assessment of polypeptide chain degradation in vivo.
    • Evaluation of cross-reacting material (CRM) levels.

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  • Examination of subunit association and protein half-life.

    • Main Results:

    • Ten out of 43 missense mutations resulted in in vivo degradation of lacZ polypeptide chains.
    • Many mutants showed reduced or absent cross-reacting material (CRM).
    • No significant correlation was observed between protein degradation and mutation map position, altered subunit association, or protein half-life.

    Conclusions:

    • In vivo degradation is a common outcome for certain lacZ missense mutations in Escherchia coli.
    • Protein degradation appears to be independent of mutation location, subunit interactions, and protein stability as measured by half-life.