Detection of an Intracellular Protease Inhibitor in Archaea |
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Authors: | María I Giménez Jorge J Sánchez Rosana E De Castro |
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Institution: | (1) Instituto de Investigaciones Biológicas, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, Casilla de Correo 1245, (7600) Mar del Plata, Argentina, AR |
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Abstract: | Proteolytic activity and a subtilisin inhibitor (NSI) were detected in Natrialba magadii cells. The proteolytic activity was due to two different proteases: a ∼90-kDa metallo protease (NMP) produced during exponential
growth and a 246-kDa serine protease (NSP) detected in the stationary phase. Both proteases were detected in the cytosolic
fraction. NSI activity was maximal during early stages of growth and decreased in the stationary phase. NSI is a 35-kDa thermosensitive
protein; it inhibits NSP activity but has no effect on NMP, and it was detected as a soluble or membrane-bound protein depending
on the growth phase. Our results suggest that NSI may regulate NSP activity in vivo and that this protease may have a role
in stationary phase cells. To our knowledge, this is the first report on the occurrence of protease inhibitors in Archaea.
Received: 4 May 2002 / Accepted: 10 July 2002 |
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