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Published on: November 12, 2012

Autolysis of a division mutant of Escherichia coli

D Karibian, G Pellon, J Starka

    Journal of General Microbiology
    |September 1, 1981
    PubMed

    Insights

    The envC Escherichia coli mutant exhibits enzyme leakage and autolysis due to altered cell envelope components. Increased L,D-carboxypeptidase activity suggests its role in septum splitting.

    Area of Science:

    • Microbiology
    • Molecular Biology
    • Biochemistry

    Background:

    • The envC gene in Escherichia coli is known to regulate cell division and morphology.
    • Mutations in envC lead to characteristic chain-forming phenotypes and potential alterations in cell wall integrity.

    Purpose of the Study:

    • To investigate the pleiotropic effects of the envC mutation in Escherichia coli.
    • To elucidate the mechanisms underlying enzyme leakage and autolysis in envC mutants.
    • To explore the role of specific murein hydrolases in envC-mediated cell lysis.

    Main Methods:

    • Characterization of periplasmic enzyme leakage in envC mutant cells.
    • Assay of various murein hydrolase activities (exo-beta-N-acetylglucosaminidase, endopeptidase, etc.) in cell extracts.
    • Growth of envC cells in high-sucrose medium to observe morphological changes and enzyme activity shifts.

    Main Results:

    • envC mutant cells showed significant leakage of periplasmic enzymes and released murein fragments.
    • Elevated exo-beta-N-acetylglucosaminidase and soluble endopeptidase activities were observed in envC cell extracts.
    • Growth in high sucrose medium induced chain separation and a substantial increase in L,D-carboxypeptidase activity.

    Conclusions:

    • The autolysis observed in envC mutants is likely triggered by alterations in envelope constituents, not solely by increased murein hydrolase activity.
    • L,D-carboxypeptidase activity appears to be involved in the septum splitting process during cell division.

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