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 language | English |
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Pages (from-to) | 1735-1756 |
Number of pages | 22 |
Journal | Biochimica et Biophysica Acta-Biomembranes |
Volume | 1778 |
Issue number | 9 |
DOIs | |
Publication status | Published - 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