General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae
| Autor: | M Sandkvist, L O Michel, L P Hough, V M Morales, M Bagdasarian, M Koomey, V J DiRita |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
DNA
Bacterial Mutant Biology medicine.disease_cause Polymerase Chain Reaction Microbiology Pilus Open Reading Frames Plasmid Bacterial Proteins Multienzyme Complexes Endopeptidases medicine Secretion Cloning Molecular Promoter Regions Genetic Vibrio cholerae Molecular Biology Deoxyribonucleases Type II secretion system Cell Membrane Chromosome Mapping Membrane Proteins Gene Expression Regulation Bacterial Sequence Analysis DNA DNA-Binding Proteins Membrane protein Multigene Family DNA Transposable Elements T-Phages Fimbriae Proteins Bacterial outer membrane Bacterial Outer Membrane Proteins Plasmids Transcription Factors Research Article |
| Zdroj: | Journal of Bacteriology. 179:6994-7003 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.179.22.6994-7003.1997 |
| Popis: | The general secretion pathway (GSP) of Vibrio cholerae is required for secretion of proteins including chitinase, enterotoxin, and protease through the outer membrane. In this study, we report the cloning and sequencing of a DNA fragment from V. cholerae, containing 12 open reading frames, epsC to -N, which are similar to GSP genes of Aeromonas, Erwinia, Klebsiella, Pseudomonas, and Xanthomonas spp. In addition to the two previously described genes, epsE and epsM (M. Sandkvist, V. Morales, and M. Bagdasarian, Gene 123: 81-86, 1993; L. J. Overbye, M. Sandkvist, and M. Bagdasarian, Gene 132:101-106, 1993), it is shown here that epsC, epsF, epsG, and epsL also encode proteins essential for GSP function. Mutations in the eps genes result in aberrant outer membrane protein profiles, which indicates that the GSP, or at least some of its components, is required not only for secretion of soluble proteins but also for proper outer membrane assembly. Several of the Eps proteins have been identified by use of the T7 polymerase-promoter system in Escherichia coli. One of them, a pilin-like protein, EpsG, was analyzed also in V. cholerae and found to migrate as two bands on polyacrylamide gels, suggesting that in this organism it might be processed or otherwise modified by a prepilin peptidase. We believe that TcpJ prepilin peptidase, which processes the subunit of the toxin-coregulated pilus, TcpA, is not involved in this event. This is supported by the observations that apparent processing of EpsG occurs in a tcpJ mutant of V. cholerae and that, when coexpressed in E. coli, TcpJ cannot process EpsG although the PilD peptidase from Neisseria gonorrhoeae can. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|