PMID:16337610

Citation	Genest, O, Seduk, F, Ilbert, M, Méjean, V and Iobbi-Nivol, C (2006) Signal peptide protection by specific chaperone. Biochem. Biophys. Res. Commun. 339:991-5
Abstract	TorD is the private chaperone of TorA, a periplasmic respiratory molybdoenzyme of Escherichia coli. In this study, it is demonstrated that TorD is required to maintain the integrity of the twin-arginine signal sequence of the cytoplasmic TorA precursors. In the absence of TorD, 35 out of the 39 amino acid residues of the signal peptide were lost and the proteolysis of the N-terminal extremity of TorA precursors was not prevented by the molybdenum cofactor insertion. We thus propose that one of the main roles of TorD is to protect the TorA signal peptide to allow translocation of the enzyme by the TAT system.
Links	PubMed Online version:10.1016/j.bbrc.2005.11.107
Keywords	Amino Acid Sequence; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Molecular Sequence Data; Oxidoreductases, N-Demethylating/chemistry; Oxidoreductases, N-Demethylating/metabolism; Protein Sorting Signals/physiology
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