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Extracellular acid proteases from Neurospora crassa.

R A Lindberg, W G Rhodes, L D Eirich

    Journal of Bacteriology
    |June 1, 1982
    PubMed
    Summary

    Neurospora crassa secretes distinct acid proteases regulated by specific nutrient limitations. This regulation differs from alkaline and neutral proteases, suggesting unique control mechanisms for these enzymes.

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    Area of Science:

    • Enzymology
    • Microbial Physiology
    • Molecular Biology

    Background:

    • Neurospora crassa produces alkaline, neutral, and acid proteases.
    • Alkaline and neutral proteases are induced by exogenous protein and secreted upon limitation of carbon, nitrogen, or sulfur.
    • Acid proteases also require protein induction but exhibit differential regulation based on specific nutrient deprivation.

    Purpose of the Study:

    • To investigate the differential regulation of acid proteases in Neurospora crassa.
    • To characterize two specific acid proteases, AcP and M-2, in response to nutrient limitation.

    Main Methods:

    • Culture filtrates of Neurospora crassa were analyzed for protease activity.
    • Enzyme induction and secretion were studied under varying nutrient limitations (carbon, nitrogen, sulfur).
    • Partial purification of AcP and M-2 was achieved using ultrafiltration, cation-exchange chromatography, and gel filtration.

    Main Results:

    • Three distinct acid proteases were identified: AcP, M-1, and M-2.
    • AcP secretion was high under sulfur limitation, low under nitrogen limitation, and undetectable under carbon limitation.
    • M-1 and M-2 showed specific secretion patterns related to nitrogen, carbon, and sulfur limitation.
    • AcP (66 kDa) is pepstatin-inhibitable, stable pH 3.0-6.0, optimal pH 4.0.
    • M-2 (18 kDa) is chelator-sensitive, stable pH 1.6-5.5, optimal pH 4.5.

    Conclusions:

    • Acid protease secretion in Neurospora crassa is differentially regulated by specific nutrient limitations, unlike alkaline and neutral proteases.
    • The regulation of acid proteases may not occur at the transcriptional level.
    • Characterization of AcP and M-2 provides insights into their distinct biochemical properties and roles.

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