Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences

TY - JOUR

T1 - Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences

AU - Jacobs, M

AU - Kontinen, V

AU - Sarvas, M

AU - Andersen, Jens Bo

PY - 1993/5

Y1 - 1993/5

N2 - In prsA (protein secretion) mutants of Bacillus subtilis, decreased levels of exoproteins, including alpha-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 alpha-amylase).

AB - In prsA (protein secretion) mutants of Bacillus subtilis, decreased levels of exoproteins, including alpha-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 alpha-amylase).

KW - Alkaline Phosphatase

KW - Bacillus subtilis

KW - Bacterial Proteins

KW - Base Sequence

KW - Chaperonins

KW - Endopeptidases

KW - Lipoproteins

KW - Molecular Sequence Data

KW - Protein Conformation

KW - Protein Folding

KW - Protein Precursors

KW - Protein Sorting Signals

KW - Proteins

KW - Recombinant Fusion Proteins

KW - Subtilisins

KW - alpha-Amylases

M3 - Journal article

C2 - 8102773

SN - 0950-382X

VL - 8

SP - 957

EP - 966

JO - Molecular Microbiology

JF - Molecular Microbiology

IS - 5

ER -