Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 270, Issue 6, Pages 1211-1221Publisher
WILEY
DOI: 10.1046/j.1432-1033.2003.03481.x
Keywords
ATP dependence; high potential iron-sulfur protein (HiPIP); in vitro folding; membrane targeting; twin arginine translocation
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Funding
- NIGMS NIH HHS [R01 GM038237, GM 38237] Funding Source: Medline
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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.
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