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- Title
Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-- sequences.
- Authors
Jacobs, M.; Andersen, J. B.; Kontinen, V.; Sarvas, M.
- Abstract
In <em>prsA</em> (protein secretion) mutants of <em>Bacillus subtilis</em>, decreased levels of exoproteins, including α-amylase and subtilisins, are found extracellularly. The effect of <em>prsA</em> on subtilisin secretion is elaborated here. Extra-cytoplasmic folding and secretion of active subtilisin is assisted by the <em>N</em>-terminal pro-sequence of its precursor. In this paper we present evidence that the product of the <em>prsA</em> gene is additionally required for these processes <em>in vivo</em>. We examined inducible expression of different subtilis--alkaline phosphatase fusion genes in the <em>prsA3</em> mutant. We found massive degradation of the fusion proteins, and a lack of enzymatic activity in the protein secreted. We suggest that <em>PrsA</em> is a novel chaperone with a predicted extracytoplasmic location, and is important <em>in vivo</em> for the proper conformation of various exoproteins, including those with pro-sequence (like subtilisin) and those without (like α-amylase).
- Subjects
BACILLUS subtilis; AMYLASES; ALKALINE phosphatase; GENES; PROTEINS
- Publication
Molecular Microbiology, 1993, Vol 8, Issue 5, p957
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.1993.tb01640.x