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Chloramphenicol acetylation in Streptomyces

W V Shaw, D A Hopwood

    Journal of General Microbiology
    |May 1, 1976
    PubMed
    Summary

    This study screened actinomycetes for chloramphenicol acetyltransferase, finding it in three Streptomyces species. Enzyme activity was higher in a resistant mutant but not inducible.

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    Area of Science:

    • Microbiology
    • Enzymology
    • Antibiotic Resistance

    Background:

    • Chloramphenicol resistance is often mediated by chloramphenicol acetyltransferase (CAT).
    • Actinomycetes are a diverse group of bacteria, with some species known to produce antibiotics.
    • Understanding the distribution and characteristics of CAT in actinomycetes is crucial for antibiotic resistance research.

    Purpose of the Study:

    • To screen various actinomycete strains for the presence and activity of chloramphenicol acetyltransferase.
    • To investigate the inducibility and specific activity of CAT in selected strains and mutants.
    • To compare CAT activity in strains related to chloramphenicol production.

    Main Methods:

    • Screening of 21 actinomycete strains for CAT activity.
    • Assaying mycelial lysates for the catalytic formation of chloramphenicol acetates using acetyl-coenzyme A.
    • Characterizing CAT activity in a chloramphenicol-resistant mutant and its parental strain.
    • Testing for enzyme inducibility under chloramphenicol exposure.

    Main Results:

    • Five strains from three species (Streptomyces coelicolor, S. acrimycini, S. griseus) exhibited CAT activity.
    • A chloramphenicol-resistant S. acrimycini mutant showed higher specific CAT activity than the wild-type.
    • The enzyme was not inducible in any tested strains or the mutant.
    • CAT activity was absent in S. venezuelae, a chloramphenicol-producing species.

    Conclusions:

    • CAT is present in specific Streptomyces species, contributing to chloramphenicol resistance.
    • Increased CAT specific activity correlates with enhanced resistance, but the enzyme is constitutively expressed.
    • The absence of CAT in S. venezuelae suggests alternative resistance mechanisms or lack thereof in this producer strain.

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