Signal peptidase I-mediated processing of an engineered mammalian cytochrome b5 precursor is an exocytoplasmic post-translocational event in Escherichia coli

Naheed N. Kaderbhai, Victoria Harding, Mustak A. Kaderbhai

Research output: Contribution to journalArticlepeer-review

6 Citations (SciVal)

Abstract

Proteins destined for translocation across the prokaryotic cytoplasmic membrane are synthesized as precursors carrying transient N-terminal extensions known as signal sequences. They facilitate initial engagement of precursor proteins with the sec-dependent translocase to initiate active threading of the polypeptide across the membrane. The translocated precursor is then processed by a transcytoplasmic signal peptidase anchored to the inner membrane. The temporal nature of cleavage of the signal sequence during pre-protein translocation has remained elusive. Using an engineered mammalian cytochrome b5 precursor we demonstrate that the signal peptide processing in Escherichia coli is an event that can occur after almost complete exocytoplasmic translocation of the preprotein is accomplished. We discuss implications of the findings in light of the known working model of sec-dependent pre-protein translocon.
Original languageEnglish
Pages (from-to)388-399
Number of pages12
JournalMolecular Membrane Biology
Volume25
Issue number5
DOIs
Publication statusPublished - 01 Aug 2008

Keywords

  • Protein translocation
  • protein targeting
  • signal sequence processing signal peptidase I
  • cytochrome b5
  • recombinant protein

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