PMID:10544036

Citation	Volkert, TL, Baleja, JD and Kumamoto, CA (1999) A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. Biochem. Biophys. Res. Commun. 264:949-54
Abstract	The Escherichia coli export chaperone SecB binds nascent precursors of certain periplasmic and outer membrane proteins and prevents them from folding or aggregating in the cytoplasm. In this study, we demonstrate that the C-terminal 13 residues of SecB were highly mobile using (1)H NMR spectroscopy. A protein lacking the C-terminal 13 amino acids of wild-type SecB was found to retain the ability to bind unfolded maltose-binding protein (MBP) in vitro but to interfere with the normal kinetics of pre-MBP export when overexpressed in vivo. The defect in export was reversed by overproduction of the peripheral membrane ATPase SecA. Therefore, deletion of the mobile region of SecB may alter the interactions of SecB with SecA.
Links	PubMed Online version:10.1006/bbrc.1999.1590
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Biological Transport; Escherichia coli; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Protein Folding
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