Abstract

The broad objective of this program is the understanding of metabolic regulation. The specific goals in the development of this program fall into three categories: (1) the understanding of molecular interactions at the purified protein level, (2) the understanding of controls in a model regulatory system, in particular the chemotactic sensory system of bacteria, and (3) the understanding of the role of the opiate receptor in the pain mechanisms of higher species. The work will involve the study of purified proteins from each of these systems, the modification of these proteins with reporter groups such as fluorescent dyes, and the study of these proteins in partially or completely reconstituted systems. It is hoped that purification of the components and the modification of their in vivo interactions will lead to greater clarification of regulatory controls in general and feedback systems in particular.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK009765-21
Application #
3224637
Study Section
Biochemistry Study Section (BIO)
Project Start
1977-12-01
Project End
1987-11-30
Budget Start
1985-12-01
Budget End
1986-11-30
Support Year
21
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Cheever, L; Koshland Jr, D E (1994) Habituation of neurosecretory responses to extracellular ATP in PC12 cells. J Neurosci 14:4831-8
Danielson, M A; Biemann, H P; Koshland Jr, D E et al. (1994) Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study. Biochemistry 33:6100-9
Jeffery, C J; Koshland Jr, D E (1994) A single hydrophobic to hydrophobic substitution in the transmembrane domain impairs aspartate receptor function. Biochemistry 33:3457-63
Biemann, H P; Koshland Jr, D E (1994) Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity. Biochemistry 33:629-34
Shapiro, M J; Koshland Jr, D E (1994) Mutagenic studies of the interaction between the aspartate receptor and methyltransferase from Escherichia coli. J Biol Chem 269:11054-9
Morimoto, B H; Koshland Jr, D E (1994) Conditional activation of cAMP signal transduction by protein kinase C. The effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells. J Biol Chem 269:4065-9
Jeffery, C J; Koshland Jr, D E (1993) Vibrio cholerae hlyB is a member of the chemotaxis receptor gene family. Protein Sci 2:1532-5
Scott, W G; Milligan, D L; Milburn, M V et al. (1993) Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium. J Mol Biol 232:555-73
Jeffery, C J; Koshland Jr, D E (1993) Three-dimensional structural model of the serine receptor ligand-binding domain. Protein Sci 2:559-66
Yeh, J I; Biemann, H P; Pandit, J et al. (1993) The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem 268:9787-92

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