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

P. Natale, T Brüser, A.J.M. Driessen

Research output: Contribution to journalReview articlepeer-review

342 Citations (Scopus)

Abstract

In bacteria, two major pathways exist to secrete proteins across the cytoplasmic membrane. The general Secretion route, termed Sec-pathway, catalyzes the transmembrame 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. (C) 2007 Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)1735-1756
Number of pages22
JournalBiochimica et Biophysica Acta-Biomembranes
Volume1778
Issue number9
DOIs
Publication statusPublished - Sept-2008

Keywords

  • secretion
  • SecA
  • SecY
  • twin arginine
  • Tat
  • ESCHERICHIA-COLI SECA
  • TWIN-ARGININE TRANSLOCASE
  • BACILLUS-SUBTILIS SECA
  • EXPORT CHAPERONE SECB
  • PROTON MOTIVE FORCE
  • ATP-BINDING-SITE
  • THYLAKOID LUMEN PROTEIN
  • AMINO-TERMINAL REGION
  • RIESKE FE/S PROTEIN
  • X-RAY-STRUCTURE

Cite this