scholarly journals The signal peptide cleavage site of a B1 hordein determined by radiosequencing of the in vitro synthesized and processed polypeptide

1989 ◽  
Vol 54 (5) ◽  
pp. 181-192 ◽  
Author(s):  
Verena Cameron-Mills ◽  
Susan M. Madrid
Keyword(s):  
Signal Peptide ◽  
Cleavage Site ◽  
Peptide Cleavage ◽  
Signal Peptide Cleavage Site

The A16V signal peptide cleavage site mutation in the cationic trypsinogen gene and chronic pancreatitis

1999 ◽  
Vol 117 (6) ◽  
pp. 1508-1509 ◽  
Author(s):  
Jian-Min Chen ◽  
Odile Raguenes ◽  
Claude Ferec ◽  
Pierre H. Deprez ◽  
Christine Verellen-Dumoulin ◽  
...  
Keyword(s):  
Chronic Pancreatitis ◽  
Signal Peptide ◽  
Cleavage Site ◽  
Site Mutation ◽  
Peptide Cleavage ◽  
Signal Peptide Cleavage Site ◽  
Cationic Trypsinogen

scholarly journals A Nine-Residue Synthetic Propeptide Enhances Secretion Efficiency of Heterologous Proteins inLactococcus lactis

1998 ◽  
Vol 180 (7) ◽  
pp. 1895-1903 ◽  
Author(s):  
Y. Le Loir ◽  
A. Gruss ◽  
S. D. Ehrlich ◽  
P. Langella
Keyword(s):  
Signal Peptide ◽  
Cleavage Site ◽  
Bacillus Stearothermophilus ◽  
Potential Candidate ◽  
Heterologous Proteins ◽  
Peptide Cleavage ◽  
Signal Peptide Cleavage Site ◽  
Secretion Efficiency ◽  
Model Protein ◽  
A Cell

ABSTRACT Lactococcus lactis, a gram-positive organism widely used in the food industry, is a potential candidate for the secretion of biologically useful proteins. We examined the secretion efficiency and capacity of L. lactis by using the Staphylococcus aureus nuclease (Nuc) as a heterologous model protein. When expressed in L. lactis from an efficient lactococcal promoter and its native signal peptide, only ∼60% of total Nuc was present in a secreted form at ∼5 mg per liter. The remaining 40% was found in a cell-associated precursor form. The secretion efficiency was reduced further to ∼30% by the deletion of 17 residues of the Nuc native propeptide (resulting in NucT). We identified a modification which improved secretion efficiency of both native Nuc and NucT. A 9-residue synthetic propeptide, LEISSTCDA, which adds two negative charges at the +2 and +8 positions, was fused immediately after the signal peptide cleavage site. In the case of Nuc, secretion efficiency was increased to ∼80% by LEISSTCDA insertion without altering the signal peptide cleavage site, and the yield was increased two- to fourfold (up to ∼20 mg per liter). The improvement of NucT secretion efficiency was even more marked and rose from 30 to 90%. Similarly, the secretion efficiency of a third protein, the α-amylase ofBacillus stearothermophilus, was also improved by LEISSTCDA. These data indicate that the LEISSTCDA synthetic propeptide improves secretion of different heterologous proteins in L. lactis.

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