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PMID: 1629152 Published · ppublish English Journal Article

Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B.

Journal of bacteriology ·Vol. 174 ·No. 15 ·1992-08-00 ·Pages 4920-7

Létoffé S, Wandersman C

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.

MeSH Terms
Adenylyl Cyclases/genetics,metabolism Amino Acid Sequence Bacterial Proteins/metabolism Bacterial Toxins/metabolism Dickeya chrysanthemi/enzymology Endopeptidases/analysis,physiology Escherichia coli/metabolism Escherichia coli Proteins Glycine/analysis Hemolysin Proteins Molecular Sequence Data Recombinant Fusion Proteins/metabolism
Chemicals
Bacterial Proteins Bacterial Toxins Escherichia coli Proteins Hemolysin Proteins Hlya protein, E coli Recombinant Fusion Proteins Endopeptidases Adenylyl Cyclases Glycine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Létoffé S
Unité de Génétique Moléculaire, Institut Pasteur (CNRS URA 1149), Paris, France.
Wandersman C
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.174.15.4920-4927.1992
Published
1992-08-00
Pages
4920-7
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC206304
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.174.15.4920-4927.1992 PMC Full Text View journal details
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