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Journal of Bacteriology, October 1999, p. 6108-6113, Vol. 181, No. 19
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

Martin H. Lee,1,dagger Nick Kosuk,1 Jeannie Bailey,1 Beth Traxler,2 and Colin Manoil1,*

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.

* 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.

dagger Present address: Division of Infectious Disease, Children's Hospital Regional Medical Center, Seattle, WA 98115.

Journal of Bacteriology, October 1999, p. 6108-6113, Vol. 181, No. 19
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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