Details
| Original language | English |
|---|---|
| Pages (from-to) | 1735-1756 |
| Number of pages | 22 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 1778 |
| Issue number | 9 |
| Publication status | Published - Sept 2008 |
| Externally published | Yes |
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.
Keywords
- SecA, Secretion, SecY, Tat, Twin arginine
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1778, No. 9, 09.2008, p. 1735-1756.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-Distinct translocases and mechanisms
AU - Natale, Paolo
AU - Brüser, Thomas
AU - Driessen, Arnold J.M.
N1 - Funding Information: This work was supported by the Council for Chemical Sciences of the Netherlands Organization for Scientific Research and subsidized by the Dutch Organization for the Advancement of Scientific Research, and NanoNed, a national nanotechnology program coordinated by the Dutch Ministry of Economic Affairs (to A.J.M.D.) and by grants of the Deutsche Forschungsgemeinschaft and the state Sachsen-Anhalt (Exzellenzcluster Biowissenschaften) to T.B. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2008/9
Y1 - 2008/9
N2 - 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.
AB - 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.
KW - SecA
KW - Secretion
KW - SecY
KW - Tat
KW - Twin arginine
UR - http://www.scopus.com/inward/record.url?scp=50049087513&partnerID=8YFLogxK
U2 - 10.1016/j.bbamem.2007.07.015
DO - 10.1016/j.bbamem.2007.07.015
M3 - Review article
C2 - 17935691
AN - SCOPUS:50049087513
VL - 1778
SP - 1735
EP - 1756
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
SN - 0005-2736
IS - 9
ER -