Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane--distinct translocases and mechanisms

Biochim Biophys Acta. 2008 Sep;1778(9):1735-56. doi: 10.1016/j.bbamem.2007.07.015. Epub 2007 Aug 9.

Abstract

In bacteria, two major pathways exist to secrete proteins across the cytoplasmic membrane. The general Secretion route, termed Sec-pathway, catalyzes the transmembrane translocation of proteins in their unfolded conformation, whereupon they fold into their native structure at the trans-side of the membrane. The Twin-arginine translocation pathway, termed Tat-pathway, catalyses the translocation of secretory proteins in their folded state. Although the targeting signals that direct secretory proteins to these pathways show a high degree of similarity, the translocation mechanisms and translocases involved are vastly different.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphatases / physiology*
  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / physiology
  • Carrier Proteins / physiology*
  • Cell Membrane / metabolism*
  • Energy Metabolism / physiology
  • Escherichia coli Proteins / physiology
  • Membrane Transport Proteins / physiology*
  • Metabolic Networks and Pathways / physiology*
  • Models, Biological
  • Models, Molecular
  • Protein Folding
  • Protein Sorting Signals / physiology
  • Protein Transport / physiology
  • SEC Translocation Channels
  • SecA Proteins

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Protein Sorting Signals
  • SEC Translocation Channels
  • twin-arginine translocase complex, E coli
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • SecA Proteins