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Penicillin-binding component of Bacillus cereus.

R F Aten, R A Day

    Journal of Bacteriology
    |May 1, 1973
    PubMed
    Summary

    Irreversibly bound penicillin in Bacillus cereus is necessary for penicillinase synthesis. This bound penicillin can be solubilized as a labile complex, suggesting a lipoprotein complex acts as the penicillin-specific binding site.

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    Detecting protein-protein interactions in the intact cell of Bacillus subtilis (ATCC 6633).

    Journal of bacteriology·2003

    Area of Science:

    • Microbiology
    • Biochemistry

    Background:

    • Bacillus cereus 569 irreversibly binds (14)C-penicillin.
    • Penicillin-treated cells release approximately 60% of bound label upon cell wall digestion.

    Purpose of the Study:

    • To investigate the role of irreversibly bound penicillin in penicillinase synthesis.
    • To characterize the nature of the penicillin-binding site in Bacillus cereus.

    Main Methods:

    • Preparation of spheroplasts from penicillin-treated Bacillus cereus using cold or 37°C treatments.
    • Incubation of spheroplasts to assess penicillinase synthesis rates and levels.
    • Chromatographic analysis of solubilized penicillin-binding complexes using Bio Gel P-150 columns.

    Main Results:

    • Spheroplasts showed reduced penicillinase synthesis compared to whole cells.
    • Spheroplasts from 37°C treatment synthesized higher penicillinase levels than those from cold treatment.
    • Solubilized penicillin-binding material was characterized, with some appearing as a labile complex excluded from Bio Gel P-150.

    Conclusions:

    • Irreversibly bound penicillin is required for induced penicillinase synthesis.
    • A labile, penicillin-binding lipoprotein complex, likely the penicillin-specific binding site, was identified.
    • The precise location of this complex relative to the cell membrane remains undetermined.

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