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A novel two‐component regulatory system in Bacillus subtilis for the survival of severe secretion stress
Author(s) -
Hyyryläinen HanneLeena,
Bolhuis Albert,
Darmon Elise,
Muukkonen Leila,
Koski Pertti,
Vitikainen Marika,
Sarvas Matti,
Prágai Zoltán,
Bron Sierd,
Van Dijl Jan Maarten,
Kontinen Vesa P.
Publication year - 2001
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 - 10.1046/j.1365-2958.2001.02576.x
Subject(s) - periplasmic space , biology , bacillus subtilis , eubacterium , cell envelope , secretion , bacterial outer membrane , sigma factor , microbiology and biotechnology , secretory protein , gene , escherichia coli , genetics , biochemistry , bacteria , rna polymerase
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 α‐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 .