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Related Experiment Videos

Bacillus licheniformis beta-lactamases: multiple forms and their roles.

J O Lampen, J B Nielsen, K Izui

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |May 16, 1980
    PubMed
    Summary

    Bacillus licheniformis 749/C produces a precursor penicillinase with an N-terminal extension, differing from previously identified forms. This study investigates the biosynthetic relationships between these distinct penicillinase variants.

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    Area of Science:

    • Microbiology
    • Molecular Biology
    • Biochemistry

    Background:

    • Bacillus licheniformis 749/C secretes penicillinase, an enzyme crucial for antibiotic resistance.
    • Multiple forms of penicillinase exist, including a secreted exoenzyme and a membrane-bound form, with differing molecular masses and N-terminal sequences.

    Purpose of the Study:

    • To characterize the N-terminal extension of the precursor penicillinase secreted by B. licheniformis 749/C.
    • To compare this precursor form with previously identified penicillinase variants.
    • To elucidate the biosynthetic interrelations among different penicillinase forms.

    Main Methods:

    • Immunoprecipitation to detect hydrophilic penicillinase precursor.
    • In-vitro protein synthesis using Escherichia coli system to translate B. licheniformis 749/C mRNA.

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  • Partial amino acid sequencing to determine N-terminal extensions.

    • Main Results:

    • A hydrophilic penicillinase precursor with an eight amino acid N-terminal extension was identified.
    • In-vitro translation yielded a hydrophobic penicillinase (34-36 kDa) with an N-terminal extension, distinct from the secreted precursor.
    • The N-terminal sequences of the precursor and in-vitro synthesized penicillinase are incompatible with the previously reported membrane-bound form.

    Conclusions:

    • The secreted penicillinase precursor differs significantly from the previously characterized membrane-bound form.
    • The findings suggest complex biosynthetic processing and interconversion of penicillinase forms in B. licheniformis.
    • Further investigation is needed to fully understand the pathway leading to the mature exoenzyme.