Autor: |
de Kort G; Department of Medical Microbiology, University Hospital, Leiden, The Netherlands., van der Bent-Klootwijk P, van Boxtel RA, van de Klundert JA |
Jazyk: |
angličtina |
Zdroj: |
FEMS microbiology letters [FEMS Microbiol Lett] 1995 Jul 15; Vol. 130 (1), pp. 63-8. |
DOI: |
10.1016/0378-1097(95)00184-7 |
Abstrakt: |
The Enterobacter cloacae outer membrane protein OmpX is involved in resistance to beta-lactams, and possesses virulence characteristics. To gain more insight into the genetic elements that are important for OmpX expression, several mutations were introduced at, and immediately upstream of, the N-terminus of the OmpX coding sequence. These mutations enabled us to delete the 5' untranslated region and the signal peptide coding sequence. The former led to decreased ompX expression, indicating an unexpected and hitherto unexplained role for this region. Deletion of the signal peptide coding sequence blocked transport across the cytoplasmic membrane, indicating that translocation of OmpX across the cytoplasmic membrane is mediated by the general secretory pathway. |
Databáze: |
MEDLINE |
Externí odkaz: |
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