Targeting and Assembly of Periplasmic and Outer-Membrane Proteins in Escherichia Coli

Annu Rev Genet. 1998;32:59-94. doi: 10.1146/annurev.genet.32.1.59.

Abstract

Escherichia coli must actively transport many of its proteins to extracytoplasmic compartments such as the periplasm and outer membrane. To perform this duty, E. coli employs a collection of Sec (secretion) proteins that catalyze the translocation of various polypeptides through the inner membrane. After translocation across the inner membrane, periplasmic and outer-membrane proteins are folded and targeted to their appropriate destinations. Here we review our knowledge of protein translocation across the inner membrane. We also discuss the various signal transduction systems that monitor extracytoplasmic protein folding and targeting, and we consider how these signal transduction systems may ultimately control these processes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Biological Transport, Active
  • Cell Membrane / metabolism
  • Cytoplasm / metabolism
  • Escherichia coli / metabolism*
  • Models, Biological
  • Protein Folding
  • Signal Transduction

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins