| Autor: |
Hyyrylainen, HL, Bolhuis, A, Darmon, E, Muukkonen, L, Koski, P, Vitikainen, M, Sarvas, M, Pragal, Z, Bron, S, van Dijl, JM, Kontinen, VP |
| Přispěvatelé: |
Groningen Biomolecular Sciences and Biotechnology, Translational Immunology Groningen (TRIGR) |
| Jazyk: |
angličtina |
| Rok vydání: |
2001 |
| Předmět: |
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| Zdroj: |
Molecular Microbiology, 41(5), 1159-1172. Wiley |
| ISSN: |
0950-382X |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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