A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress.
Mol Microbiol
; 41(5): 1159-72, 2001 Sep.
Article
in En
| MEDLINE
| ID: mdl-11555295
ABSTRACT
The Gram-positive eubacterium Bacillus subtilis is well known for its high capacity to secrete proteins into the environment. Even though high-level secretion of proteins is an efficient process, it imposes stress on the cell. The present studies were aimed at the identification of systems required to combat this so-called secretion stress. A two-component regulatory system, named CssR-CssS, was identified, which bears resemblance to the CpxR-CpxA system of Escherichia coli. The results show that the CssR/S system is required for the cell to survive the severe secretion stress caused by a combination of high-level production of the alpha-amylase AmyQ and reduced levels of the extracytoplasmic folding factor PrsA. As shown with a prsA3 mutation, the Css system is required to degrade misfolded exported proteins at the membrane-cell wall interface. This view is supported by the observation that transcription of the htrA gene, encoding a predicted membrane-bound protease of B. subtilis, is strictly controlled by CssS. Notably, CssS represents the first identified sensor for extracytoplasmic protein misfolding in a Gram-positive eubacterium. In conclusion, the results show that quality control systems for extracytoplasmic protein folding are not exclusively present in the periplasm of Gram-negative eubacteria, but also in the Gram-positive cell envelope.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacillus subtilis
/
Bacterial Proteins
/
Gene Expression Regulation, Bacterial
/
Periplasmic Proteins
/
Alpha-Amylases
/
Heat-Shock Proteins
Type of study:
Prognostic_studies
Language:
En
Journal:
Mol Microbiol
Journal subject:
BIOLOGIA MOLECULAR
/
MICROBIOLOGIA
Year:
2001
Document type:
Article
Affiliation country:
Finland