Details
| Original language | English |
|---|---|
| Pages (from-to) | 1211-1221 |
| Number of pages | 11 |
| Journal | European Journal of Biochemistry |
| Volume | 270 |
| Issue number | 6 |
| Publication status | Published - Mar 2003 |
| Externally published | Yes |
Abstract
Targeting of proteins to and translocation across the membranes is a fundamental biological process in all organisms. In bacteria, the twin arginine translocation (Tat) system can transport folded proteins. Here, we demonstrate in vivo that the high potential iron-sulfur protein (HiPIP) from Allochromatium vinosum is translocated into the periplasmic space by the Tat system of Escherichia coli. In vitro, reconstituted HiPIP precursor (preHoloHiPIP) was targeted to inverted membrane vesicles from E. coli by a process requiring ATP when the Tat substrate was properly folded. During membrane targeting, the protein retained its cofactor, indicating that it was targeted in a folded state. Membrane targeting did not require a twin arginine motif and known Tat system components. On the basis of these findings, we propose that a pathway exists for the insertion of folded cofactor-containing proteins such as HiPIP into the bacterial cytoplasmic membrane.
Keywords
- ATP dependence, High potential iron-sulfur protein (HiPIP), In vitro folding, Membrane targeting, Twin arginine translocation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
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In: European Journal of Biochemistry, Vol. 270, No. 6, 03.2003, p. 1211-1221.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Membrane targeting of a folded and cofactor-containing protein
AU - Brüser, Thomas
AU - Yano, Takahiro
AU - Brune, Daniel C.
AU - Daldal, Fevzi
N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2003/3
Y1 - 2003/3
N2 - Targeting of proteins to and translocation across the membranes is a fundamental biological process in all organisms. In bacteria, the twin arginine translocation (Tat) system can transport folded proteins. Here, we demonstrate in vivo that the high potential iron-sulfur protein (HiPIP) from Allochromatium vinosum is translocated into the periplasmic space by the Tat system of Escherichia coli. In vitro, reconstituted HiPIP precursor (preHoloHiPIP) was targeted to inverted membrane vesicles from E. coli by a process requiring ATP when the Tat substrate was properly folded. During membrane targeting, the protein retained its cofactor, indicating that it was targeted in a folded state. Membrane targeting did not require a twin arginine motif and known Tat system components. On the basis of these findings, we propose that a pathway exists for the insertion of folded cofactor-containing proteins such as HiPIP into the bacterial cytoplasmic membrane.
AB - Targeting of proteins to and translocation across the membranes is a fundamental biological process in all organisms. In bacteria, the twin arginine translocation (Tat) system can transport folded proteins. Here, we demonstrate in vivo that the high potential iron-sulfur protein (HiPIP) from Allochromatium vinosum is translocated into the periplasmic space by the Tat system of Escherichia coli. In vitro, reconstituted HiPIP precursor (preHoloHiPIP) was targeted to inverted membrane vesicles from E. coli by a process requiring ATP when the Tat substrate was properly folded. During membrane targeting, the protein retained its cofactor, indicating that it was targeted in a folded state. Membrane targeting did not require a twin arginine motif and known Tat system components. On the basis of these findings, we propose that a pathway exists for the insertion of folded cofactor-containing proteins such as HiPIP into the bacterial cytoplasmic membrane.
KW - ATP dependence
KW - High potential iron-sulfur protein (HiPIP)
KW - In vitro folding
KW - Membrane targeting
KW - Twin arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=0142065248&partnerID=8YFLogxK
U2 - 10.1046/j.1432-1033.2003.03481.x
DO - 10.1046/j.1432-1033.2003.03481.x
M3 - Article
C2 - 12631279
AN - SCOPUS:0142065248
VL - 270
SP - 1211
EP - 1221
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 6
ER -