PMID:17901208
| Citation |
Maillard, J, Spronk, CA, Buchanan, G, Lyall, V, Richardson, DJ, Palmer, T, Vuister, GW and Sargent, F (2007) Structural diversity in twin-arginine signal peptide-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 104:15641-6 |
|---|---|
| Abstract |
The twin-arginine transport (Tat) system is dedicated to the translocation of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat system by signal peptides containing a twin-arginine motif. In Escherichia coli, many Tat substrates bind redox-active cofactors in the cytoplasm before transport. Coordination of cofactor insertion with protein export involves a "Tat proofreading" process in which chaperones bind twin-arginine signal peptides, thus preventing premature export. The initial Tat signal-binding proteins described belonged to the TorD family, which are required for assembly of N- and S-oxide reductases. Here, we report that E. coli NapD is a Tat signal peptide-binding chaperone involved in biosynthesis of the Tat-dependent nitrate reductase NapA. NapD binds tightly and specifically to the NapA twin-arginine signal peptide and suppresses signal peptide translocation activity such that transport via the Tat pathway is retarded. High-resolution, heteronuclear, multidimensional NMR spectroscopy reveals the 3D solution structure of NapD. The chaperone adopts a ferredoxin-type fold, which is completely distinct from the TorD family. Thus, NapD represents a new family of twin-arginine signal-peptide-binding proteins. |
| Links |
PubMed PMC2000414 Online version:10.1073/pnas.0703967104 |
| Keywords |
Arginine/metabolism; Binding Sites; Carrier Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Genetic Variation; Membrane Transport Proteins/metabolism; Nitrate Reductase/metabolism; Oxidation-Reduction; Protein Binding; Protein Sorting Signals/physiology; Signal Transduction; Substrate Specificity |
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