Prolipoprotein signal peptidase of Escherichia coli requires a cysteine residue at the cleavage site.

AUTOR(ES)

Inouye, S

RESUMO

A signal peptidase specifically required for the secretion of the lipoprotein of the Escherichia coli outer membrane cleaves off the signal peptide at the bond between a glycine and a cysteine residue. This cysteine residue was altered to a glycine residue by guided site-specific mutagenesis using a synthetic oligonucleotide and a plasmid carrying an inducible lipoprotein gene. The induction of mutant lipoprotein production was lethal to the cells. A large amount of the prolipoprotein was accumulated in the outer membrane fraction. No protein of the size of the mature lipoprotein was detected. These results indicate that the prolipoprotein signal peptidase requires a glyceride modified cysteine residue at the cleavage site.

Documentos Relacionados

• Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene.
• A Truncated Soluble Bacillus Signal Peptidase Produced in Escherichia coli Is Subject to Self-Cleavage at Its Active Site
• Efficient cleavage of pre-tRNAs by E. coli RNAse P RNA requires the 2'-hydroxyl of the ribose at the cleavage site.
• SecY, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site.
• A re-investigation of the thio effect at the hammerhead cleavage site.