Abstract
Soluble factors participate in protein translocation across a variety of biological membranes. The Escherichia coli soluble protein SecB (the product of the secB gene) is involved in the export of periplasmic and outer membrane proteins. The isolation of secB mutations permitted the demonstration that SecB is required for rapid and efficient export of certain proteins. Consistent with the results of these genetic studies, purified SecB has been shown to stimulate protein translocation across E. coli inner membrane vesicles in vitro. This article presents a review of these past studies of SecB, speculation on the role of SecB in protein translocation, and a comparison of SecB and other factors, trigger factor and GroEL.
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