PMID:15941830
| Citation |
Hatzixanthis, K, Clarke, TA, Oubrie, A, Richardson, DJ, Turner, RJ and Sargent, F (2005) Signal peptide-chaperone interactions on the twin-arginine protein transport pathway. Proc. Natl. Acad. Sci. U.S.A. 102:8460-5 |
|---|---|
| Abstract |
The twin-arginine transport (Tat) system is a protein-targeting pathway of prokaryotes and chloroplasts. Most Escherichia coli Tat substrates are complex metalloenzymes that must be correctly folded and assembled before transport, and a preexport chaperone-mediated "proofreading" process is therefore in operation. The paradigm proofreading chaperone is TorD, which coordinates maturation and export of the key respiratory enzyme trimethylamine N-oxide reductase (TorA). It is demonstrated here that purified TorD binds tightly and with exquisite specificity to the TorA twin-arginine signal peptide in vitro. It is also reported that the TorD family constitutes a hitherto unexpected class of nucleotide-binding proteins. The affinity of TorD for GTP is enhanced by initial signal peptide binding, and it is proposed that GTP governs signal peptide binding-and-release cycles during Tat proofreading. |
| Links |
PubMed PMC1143606 Online version:10.1073/pnas.0500737102 |
| Keywords |
Amino Acid Sequence; Blotting, Western; Calorimetry; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins/metabolism; Fluorometry; Guanosine Triphosphate/metabolism; Membrane Transport Proteins/metabolism; Metalloendopeptidases/metabolism; Models, Molecular; Molecular Chaperones/metabolism; Molecular Sequence Data; Oxidoreductases, N-Demethylating/genetics; Oxidoreductases, N-Demethylating/metabolism; Plasmids/genetics; Protein Binding; Protein Sorting Signals/genetics; Protein Sorting Signals/physiology; Signal Transduction/physiology; Ultracentrifugation |
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