In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli.

Abstract excerpt

By using an in vitro system for the translocation of secretory proteins in Escherichia coli, detailed and quantitative studies were performed as to the function of the positively charged amino acid residues at the amino terminus of the signal peptide. Uncleavable OmpF-Lpp, a model secretory protein carrying an uncleavable signal peptide, and mutant proteins derived from it were used as translocation substrates....

Topics

• Amino Acid Sequence
• Arginine
• Bacterial Outer Membrane Proteins
• Bacterial Proteins
• Base Sequence
• Biological Transport
• Cell Membrane
• Cytoplasm
• Electrochemistry
• Escherichia coli