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Journal of Bacteriology, October 1999, p. 6108-6113, Vol. 181, No. 19
Departments of
Genetics1 and
Microbiology,2 University of Washington,
Seattle, Washington 98195-7360
Received 7 April 1999/Accepted 28 July 1999
This report describes a procedure for characterizing membrane
protein topology which combines the analysis of reporter protein hybrids and trypsin-sensitive 31-amino-acid insertions generated by
using transposons ISphoA/in and ISlacZ/in.
Studies of the F factor TraD protein imply that the protein takes on a
structure with two membrane-spanning sequences and amino and carboxyl
termini facing the cytoplasm. It was possible to assign the subcellular location of one region for which the behavior of fused reporter proteins was ambiguous, based on the trypsin cleavage behavior of a
31-residue insertion.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Analysis of F Factor TraD Membrane Topology by Use
of Gene Fusions and Trypsin-Sensitive Insertions

*
Corresponding author. Mailing address: Department of
Genetics, Box 357360, University of Washington, Seattle, WA 98195-7360. Phone: (206) 543-7800. Fax: (206) 543-0754. E-mail:
manoil{at}u.washington.edu.
Present address: Division of Infectious Disease, Children's
Hospital Regional Medical Center, Seattle, WA 98115.
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