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Extracellular enzyme secretion by Pseudomonas lemoignei.

M W Stinson, J M Merrick

    Journal of Bacteriology
    |July 1, 1974
    PubMed
    Summary
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    Succinate represses poly-beta-hydroxybutyrate depolymerase secretion in Pseudomonas lemoignei, but only at pH 7.0 or below. This pH-dependent repression suggests messenger RNA accumulation influences enzyme secretion.

    Area of Science:

    • Microbiology
    • Enzymology
    • Molecular Biology

    Background:

    • Pseudomonas lemoignei produces poly-beta-hydroxybutyrate depolymerase, an extracellular enzyme.
    • Regulation of bacterial exoenzyme secretion is crucial for microbial physiology and interactions.

    Purpose of the Study:

    • To investigate the influence of pH and succinate on poly-beta-hydroxybutyrate depolymerase secretion.
    • To elucidate the mechanisms underlying the regulation of depolymerase secretion.

    Main Methods:

    • Culturing Pseudomonas lemoignei under varying pH conditions.
    • Assessing enzyme secretion in response to succinate addition.
    • Utilizing inhibitors like rifampin and chloramphenicol to study synthesis and secretion pathways.

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    Main Results:

    • Succinate repressed depolymerase secretion only at pH 7.0 or lower.
    • A 30-minute delay in secretion inhibition was observed after pH shift or rifampin addition.
    • De novo protein synthesis is required for secretion; enzyme is not released from a preformed pool.
    • Exoenzyme synthesis is more sensitive to protein synthesis inhibitors than cell-associated proteins.

    Conclusions:

    • The pH of the medium significantly modulates succinate's ability to repress depolymerase secretion.
    • Evidence suggests that accumulated depolymerase messenger RNA contributes to post-repression enzyme secretion.
    • Secretion of poly-beta-hydroxybutyrate depolymerase is dependent on active synthesis and is not from a stored pool.