Premium
Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro‐sequences
Author(s) -
Jacobs M.,
Andersen J. B.,
Kontinen V.,
Sarvas M.
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01640.x
Subject(s) - subtilisin , bacillus subtilis , biology , secretion , biochemistry , mutant , chaperone (clinical) , enzyme , secretory protein , maltose binding protein , fusion protein , gene , recombinant dna , genetics , bacteria , medicine , pathology
Summary In prsA (protein secretion) mutants of Bacillus subtilis , decreased levels of exoproteins, including α‐amylase and subtilisins, are found extracellularly. The effect of prsA on subtilisin secretion is elaborated here. Extracytoplasmic folding and secretion of active subtilisin is assisted by the N ‐terminal pro‐sequence of its precursor. In this paper we present evidence that the product of the prsA gene is additionally required for these processes in vivo. We examined inducible expression of different subtilisin‐alkaline phosphatase fusion genes in the prsA3 mutant. We found massive degradation of the fusion proteins, and a lack of enzymatic activity in the protein secreted. We suggest that PrsA is a novel chaperone with a predicted extracytoplasmic location, and is important in vivo for the proper conformation of various exoproteins, including those with pro‐sequence (like subtilisin) and those without (like α‐amylase).