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Journal of Bacteriology, July 2000, p. 4108-4112, Vol. 182, No. 14
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.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
SecB Dependence of an Exported Protein Is a Continuum Influenced
by the Characteristics of the Signal Peptide or Early Mature
Region
*
Corresponding author. Mailing address: Department of
Molecular and Cell Biology, Box U-44, University of Connecticut,
Storrs, CT 06269. Phone: (860) 486-1891. Fax: (860) 486-1784. E-mail: kendall{at}uconnvm.uconn.edu.
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