title: Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B.
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.
authors.affiliation: Unité de Génétique Moléculaire, Institut Pasteur (CNRS URA 1149), Paris, France.
authors.forename: S
authors.initials: S
authors.lastname: Létoffé
authors.forename: C
authors.initials: C
authors.lastname: Wandersman
mesh_terms: D000262:Adenylyl Cyclases / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism*; D016974:Dickeya chrysanthemi / Q000201:enzymology*; D010450:Endopeptidases / Q000032:analysis / Q000502:physiology*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005998:Glycine / Q000032:analysis; D006460:Hemolysin Proteins; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; C036507:Hlya protein, E coli; D011993:Recombinant Fusion Proteins; D010450:Endopeptidases; D000262:Adenylyl Cyclases; D005998:Glycine