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Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B
- Source :
- Journal of Bacteriology. 174:4920-4927
- Publication Year :
- 1992
- Publisher :
- American Society for Microbiology, 1992.
-
Abstract
- Protease B from Erwinia chrysanthemi was shown previously to have a C-terminal secretion signal located downstream of a domain that contains six glycine-rich repeats. This domain is conserved in all known bacterial proteins secreted by the signal peptide-independent pathway. The role of these repeats in the secretion process is controversial. We compared the secretion processes of various heterologous polypeptides fused either directly to the signal or separated from it by the glycine-rich domain. Although the repeats are not involved in the secretion of small truncated protease B carboxy-terminal peptides, they are required for the secretion of higher-molecular-weight fusion proteins. Secretion efficiency was also dependent on the size of the passenger polypeptide.
- Subjects :
- Recombinant Fusion Proteins
medicine.medical_treatment
Bacterial Toxins
Molecular Sequence Data
Glycine
Pectobacterium chrysanthemi
Biology
Hemolysin Proteins
medicine.disease_cause
Microbiology
Bacterial Proteins
Endopeptidases
Escherichia coli
medicine
Secretion
Amino Acid Sequence
Molecular Biology
Peptide sequence
Protease
Escherichia coli Proteins
Dickeya chrysanthemi
cyaA
Fusion protein
Biochemistry
Adenylyl Cyclases
Research Article
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 174
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....8549593abd08f58724b328a0c3fd2b81