Two-stage model for integration of the lysis protein E of ΦX174 into the cell envelope ofEscherichia coli
| Autor: | Petra Schön, Werner Lubitz, Angela Witte, Gerald Schrot, Gerhard Wanner |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Vesicle-associated membrane protein 8
Lysis Protein Conformation Serine Endopeptidases Bacteriophage phi X174 Membrane Proteins Biology Microbiology Fusion protein Viral Proteins Bacteriolysis Infectious Diseases Protein structure Biochemistry Escherichia coli Biophysics Inner membrane Endopeptidase K Cell envelope Bacterial outer membrane Bacteriophage phi X 174 |
| Zdroj: | FEMS Microbiology Reviews. 17:207-212 |
| ISSN: | 1574-6976 |
| DOI: | 10.1111/j.1574-6976.1995.tb00203.x |
| Popis: | As a tool for determining the topology of the small, 91-amino acid phi X174 lysis protein E within the envelope complex of Escherichia coli, a lysis active fusion of protein E with streptavidin (E-FXa-StrpA) was used. The E-FXa-StrpA fusion protein was visualised using immune electron microscopy with gold-conjugated anti-streptavidin antibodies within the envelope complex in different orientations. At the distinct areas of lysis characteristic for protein E, the C-terminal end of the fusion protein was detected at the surface of the outer membrane, whereas at other areas the C-terminal portion of the protein was located at the cytoplasmic side of the inner membrane. These results suggest that a conformational change of protein E is necessary to induce the lysis process, an assumption supported by proteinase K protection studies. The immune electron microscopic data and the proteinase K accessibility studies of the E-FXa-StrA fusion protein were used for the working model of the E-mediated lysis divided into three phases: phase 1 is characterised by integration of protein E into the inner membrane without a cytoplasmic status in a conformation with its C-terminal part facing the cytoplasmic side; phase 2 is characterised by a conformational change of the protein transferring the C-terminus across the inner membrane; phase 3 is characterised by a fusion of the inner and outer membranes and is associated with a transfer of the C-terminal domain of protein E towards the surface of the outer membrane of E. coli. |
| Databáze: | OpenAIRE |
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