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PMID:12634326
| Citation |
Wahlström, E, Vitikainen, M, Kontinen, VP and Sarvas, M (2003) The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis. Microbiology (Reading, Engl.) 149:569-77 |
|---|---|
| Abstract |
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 alpha-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. |
| Links |
PubMed Online version:10.1099/mic.0.25511-0 |
| Keywords |
Bacillus subtilis/genetics; Bacillus subtilis/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/secretion; Cell Wall; Cytoplasm/metabolism; Gene Expression Regulation, Bacterial; Lipoproteins/genetics; Lipoproteins/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Protein Folding; Protoplasts/metabolism; alpha-Amylases/genetics; alpha-Amylases/secretion |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
Contributes to |
GO:0009306: protein secretion |
ECO:0000315: |
P |
The protein being tested AmyQ shows a lower concentration in the cell with the prsA3 mutation then compared to the wild type. Figure 2. |
complete | |||
Notes
See also
References
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