A signal peptide with a proline next to the cleavage site inhibits leader peptidase when present in a sec-independent protein.

Abstract excerpt

Proline residues are rarely found in the three most C-terminal positions of bacterial signal peptides, and have never been found in position +1 immediately following the cleavage site. It was recently shown that a Pro+1 mutation in the E. coli maltose binding protein precursor not only prevents cleavage of the signal peptide but also inhibits the leader peptidase enzyme, resulting in cessation of cell growth...

Topics

• Amino Acid Sequence
• Biological Transport, Active
• Consensus Sequence
• Endopeptidases
• Escherichia coli
• Membrane Proteins
• Molecular Sequence Data
• Mutation
• Proline
• Protein Processing, Post-Translational
• Protein Sorting Signals