TAILIEUCHUNG - Báo cáo khoa học: Membrane targeting of a folded and cofactor-containing protein

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 vinosumis trans-located 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. . | Eur. J. Biochem. 270 1211-1221 2003 FEBS 2003 doi Membrane targeting of a folded and cofactor-containing protein Thomas Briiser1 Takahiro Yano2 Daniel C. Brune3 and Fevzi Daldal1 2 1 Department of Biology University of Pennsylvania Philadelphia PA 19104-6018 USA 2 Johnson Research Foundation Department of Biochemistry and Biophysics University of Pennsylvania Philadelphia PA 19104-6059 USA 3Department of Chemistry and Biochemistry Arizona State University Tempe AZ 85287-1604 USA 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 cofactorcontaining proteins such as HiPIP into the bacterial cytoplasmic membrane. Keywords ATP dependence iggh pt l nii al unm-uufiur protein HiPIP in vitro folding membrane targeting twin arginine translocation. Bacteria translocate proteins across the cytoplasmic membrane by two main pathways the general secretory Sec and the twin arginine translocation Tat systems 1 2 . In the past most studies on protein targeting have focused on translocation or membrane integration of unfolded protein substrates by the Sec machinery and many components have been identified that play specific roles in Sec-dependent .

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