Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM053259-10
Application #
2192597
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1986-12-01
Project End
1998-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
10
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of Minnesota Twin Cities
Department
Miscellaneous
Type
Schools of Arts and Sciences
DUNS #
168559177
City
Minneapolis
State
MN
Country
United States
Zip Code
55455

  Publications

Johnson, J L; Brooker, R J (2004) Control of H+/lactose coupling by ionic interactions in the lactose permease of Escherichia coli. J Membr Biol 198:135-46
Green, Aileen L; Hrodey, Heather A; Brooker, Robert J (2003) Evidence for structural symmetry and functional asymmetry in the lactose permease of Escherichia coli. Biochemistry 42:11226-33
Patzlaff, Jason S; Zhang, Jingyan; Brooker, Robert J et al. (2002) An isotope-edited FT-IR study of a symporter, the lactose permease. Biochemistry 41:7366-72
Green, A L; Brooker, R J (2001) A face on transmembrane segment 8 of the lactose permease is important for transport activity. Biochemistry 40:12220-9
Pazdernik, N J; Matzke, E A; Jessen-Marshall, A E et al. (2000) Roles of charged residues in the conserved motif, G-X-X-X-D/E-R/K-X-G-[X]-R/K-R/K, of the lactose permease of Escherichia coli. J Membr Biol 174:31-40
Patzlaff, J S; Brooker, R J; Barry, B A (2000) A reaction-induced fourier transform-infrared spectroscopic study of the lactose permease. A transmembrane potential perturbs carboxylic acid residues. J Biol Chem 275:28695-700
Green, A L; Anderson, E J; Brooker, R J (2000) A revised model for the structure and function of the lactose permease. Evidence that a face on transmembrane segment 2 is important for conformational changes. J Biol Chem 275:23240-6
Johnson, J L; Brooker, R J (1999) A K319N/E325Q double mutant of the lactose permease cotransports H+ with lactose. Implications for a proposed mechanism of H+/lactose symport. J Biol Chem 274:4074-81
Patzlaff, J S; Moeller, J A; Barry, B A et al. (1998) Fourier transform infrared analysis of purified lactose permease: a monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange. Biochemistry 37:15363-75
Pazdernik, N J; Cain, S M; Brooker, R J (1997) An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner. J Biol Chem 272:26110-6

Showing the most recent 10 out of 15 publications