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Intergeneric complementation of anthranilate synthase subunits.

N Patel, W M Holmes, J F Kane

    Journal of Bacteriology
    |May 1, 1973
    PubMed
    Summary
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    Subunits of anthranilate synthase from Bacillus subtilis and Pseudomonas aeruginosa show cross-species complementation. The interaction between large and small subunits indicates functional compatibility between these bacterial species.

    Area of Science:

    • Biochemistry
    • Microbiology
    • Enzymology

    Background:

    • Anthranilate synthase is a key enzyme in the tryptophan biosynthesis pathway.
    • Enzyme function can be studied through subunit interactions and complementation assays.

    Purpose of the Study:

    • To investigate the subunit interactions of anthranilate synthase from Bacillus subtilis and Pseudomonas aeruginosa.
    • To determine the functional compatibility of heterologous subunit combinations.

    Main Methods:

    • Preparation of partially purified anthranilate synthase subunits from B. subtilis and P. aeruginosa.
    • Complementation assays using homologous and heterologous subunit mixtures.
    • Enzyme activity measurements of reconstituted complexes.

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    Main Results:

    • The large subunit from B. subtilis (I(B)) effectively complements the small subunit from P. aeruginosa (II(P)).
    • The heterologous complex I(B)II(P) exhibited 93% activity compared to the homologous complex I(B)II(B).
    • The reciprocal heterologous complex I(P)II(B) showed significantly lower activity (22%) compared to the homologous complex I(P)II(P).

    Conclusions:

    • There is functional cross-complementation between anthranilate synthase subunits from B. subtilis and P. aeruginosa.
    • The subunit interfaces exhibit differential compatibility, with I(B)II(P) being highly functional but I(P)II(B) being less so.