Journal of Bacteriology, July 2000, p. 4108-4112, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269,1 and Department of Microbiology, Institute of Molecular Biological Sciences, Biocentrum Amsterdam, 1081 HV Amsterdam, The Netherlands2
Received 2 February 2000/Accepted 2 May 2000
We have used Escherichia coli alkaline phosphatase to show the interplay among the characteristics of two amino-terminal domains in the preprotein (the signal peptide and the early mature region), the efficiency with which this protein is transported, and its requirement for SecB to accomplish the transport process. The results suggest that although alkaline phosphatase does not normally require SecB for transport, it is inherently able to utilize SecB, and it does so when its ability to interface with the transport machinery is compromised.
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