The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis

• Published in: Microbiology (Society for General Microbiology) 2003-03, Vol.149 (3), p.569-577
• Main Authors: Wahlstrom, Eva, Vitikainen, Marika, Kontinen, Vesa P, Sarvas, Matti
• Format: Article
• Language: English
• Subjects: alpha-Amylases - genetics; alpha-Amylases - metabolism; Bacillus subtilis; Bacillus subtilis - genetics; Bacillus subtilis - metabolism; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; Cell Wall; Cytoplasm - metabolism; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Bacterial; General aspects; Lipoproteins - genetics; Lipoproteins - metabolism; Mathematics in biology. Statistical analysis. Models. Metrology. Data processing in biology (general aspects); Membrane Proteins - genetics; Membrane Proteins - metabolism; Microbiology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Protein Folding; Protoplasts - metabolism; PrsA protein
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/mic.0.25511-0

Vaccine Development Laboratory, National Public Health Institute, Mannerheimintie 166, FIN-00300, Helsinki, Finland Correspondence Vesa P. Kontinen vesa.kontinen{at}ktl.fi Pulse–chase labelling was used to study the role of the cell wall microenvironment in the functioning of Bacillus subtilis PrsA, an extracellular lipoprotein and member of the parvulin family of peptidylprolyl cis / trans -isomerases. It was found that in protoplasts, and thus in the absence of a cell wall matrix, the post-translocational folding, stability and secretion of the AmyQ -amylase were independent of PrsA, in contrast to the strict dependency found in rods. The results indicate that PrsA is dedicated to assisting the folding and stability of exported proteins in the particular microenvironment of the cytoplasmic membrane–cell wall interface, possibly as a chaperone preventing unproductive interactions with the wall. The data also provide evidence for a crucial role of the wall in protein secretion. The presence of the wall directly or indirectly facilitates the release of AmyQ from the cell membrane and affects the rate of the signal peptide processing. Abbreviations: PPIase; peptidylprolyl cis / trans -isomerases; SMS, Spizizen's minimal salts Present address: Institute of Biotechnology, Biocentre 1, PO Box 56, FIN-00014 University of Helsinki, Helsinki, Finland.