Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM046493-05
Application #
2183982
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1991-07-01
Project End
1998-11-30
Budget Start
1995-12-01
Budget End
1996-11-30
Support Year
5
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Washington
Department
Genetics
Type
Schools of Arts and Sciences
DUNS #
135646524
City
Seattle
State
WA
Country
United States
Zip Code
98195
Lee, M H; Kosuk, N; Bailey, J et al. (1999) Analysis of F factor TraD membrane topology by use of gene fusions and trypsin-sensitive insertions. J Bacteriol 181:6108-13
Bailey, J; Manoil, C (1998) Missense mutations that inactivate Escherichia coli lac permease. J Mol Biol 277:199-213
Nelson, B D; Manoil, C; Traxler, B (1997) Insertion mutagenesis of the lac repressor and its implications for structure-function analysis. J Bacteriol 179:3721-8
Manoil, C; Bailey, J (1997) A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease. J Mol Biol 267:250-63
Lee, M H; Manoil, C (1997) Engineering trypsin-sensitive sites in a membrane transport protein. Protein Eng 10:715-23
Seligman, L; Bailey, J; Manoil, C (1995) Sequences determining the cytoplasmic localization of a chemoreceptor domain. J Bacteriol 177:2315-20
Seligman, L; Manoil, C (1994) An amphipathic sequence determinant of membrane protein topology. J Biol Chem 269:19888-96
Lee, E; Manoil, C (1994) Mutations eliminating the protein export function of a membrane-spanning sequence. J Biol Chem 269:28822-8
Kimbrough, T G; Manoil, C (1994) Role of a small cytoplasmic domain in the establishment of serine chemoreceptor membrane topology. J Bacteriol 176:7118-20