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J Biol Chem, Vol. 273, Issue 19, 11409-11412, May 8, 1998
From the Department of Molecular and Cell Biology, The
University of Connecticut, Storrs, Connecticut 06269
Although it is known that virtually all exported
proteins require a signal peptide, it is not clearly understood how the
signal peptide interfaces with the translocation machinery to achieve transport. In this study we document a direct interaction between the
signal peptide and SecA, a primary component of the translocase in
Escherichia coli, and show that the signal peptide itself
can stimulate SecA-lipid ATPase activity. Using synthetic signal
peptides corresponding to the wild type alkaline phosphatase signal
sequence and two model sequences, we find that the extent of
stimulation of SecA ATPase activity by the different peptides parallels
the hierarchy of results found for in vivo function (Izard,
J. W., Doughty, M. B., and Kendall, D. A. (1995)
Biochemistry 34, 9904-9912). The peptide-induced activity
requires a lipid to protein molar ratio of at least 300:1 and liposomes
enriched in negatively charged phospholipids. Furthermore, specific
binding of the signal peptide to SecA was demonstrated using chemical
cross-linking and competition with unlabeled peptides.
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