Article
A positive residue in the hydrophobic core of the Escherichia coli lipoprotein signal peptide suppresses the secretion defect caused by an acidic amino terminus.
The Journal of biological chemistry - 15 Jan 1992
Sung C Y, Gennity J M, Pollitt N S, Inouye M
Abstract excerpt
The signal peptide of secretory proteins requires a basic amino terminus followed by a stretch of hydrophobic residues to effect efficient translocation of precursor proteins. Replacement of the positively charged amino-terminal residues of prolipoprotein by acidic amino acids decreased the rate...
Topics
- Amino Acid Sequence
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Lipoproteins
- Molecular Sequence Data
- Mutation
- Plasmids
- Protein Sorting Signals