Abstract
Bacillus subtilis protease inhibitor activity increases markedly at the end of growth and during sporulation an increasing fraction of the activity was released from cells. The inhibitor is unique in its amino acid composition and the proteases affected. It is rather selective for a major B. subtilis intracellular protease and could thus have a role in modulating protease activity during sporulation but it was also active on some fungal proteases. A substantial fraction was released from protoplasts implying a surface location. While there may be localization at or near the membrane, the mechanism or site(s) probably differs from that of alkaline phosphatase and penicillinase. The inhibitor protein gene has been cloned in λgtll and subcloned in a B. subtilis integration vehicle. One subclone lacked inhibitor activity but still sporulated. A role in modulating other intracellular processes or in cell protection are still possible.
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© 1987 Plenum Press, New York
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Aronson, A.I. (1987). Formation and Properties of a Bacillus Subtilis Protein Protease Inhibitor. In: Chaloupka, J., Krumphanzl, V. (eds) Extracellular Enzymes of Microorganisms. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1274-1_12
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DOI: https://doi.org/10.1007/978-1-4684-1274-1_12
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-1276-5
Online ISBN: 978-1-4684-1274-1
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