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 Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM009765-20
Application #
3150762
Study Section
Biochemistry Study Section (BIO)
Project Start
1977-12-01
Project End
1987-11-30
Budget Start
1984-12-01
Budget End
1985-11-30
Support Year
20
Fiscal Year
1985
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

Newton, A C; Koshland Jr, D E (1990) Phosphatidylserine affects specificity of protein kinase C substrate phosphorylation and autophosphorylation. Biochemistry 29:6656-61
Newton, A C; Koshland Jr, D E (1989) High cooperativity, specificity, and multiplicity in the protein kinase C-lipid interaction. J Biol Chem 264:14909-15
Mochly-Rosen, D; Koshland Jr, D E (1988) A general procedure for screening inhibitory antibodies: application for identifying anti-protein kinase C antibodies. Anal Biochem 170:31-7
Milligan, D L; Koshland Jr, D E (1988) Site-directed cross-linking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. J Biol Chem 263:6268-75
Mochly-Rosen, D; Basbaum, A I; Koshland Jr, D E (1987) Distinct cellular and regional localization of immunoreactive protein kinase C in rat brain. Proc Natl Acad Sci U S A 84:4660-4
Newton, A C; Koshland Jr, D E (1987) Protein kinase C autophosphorylates by an intrapeptide reaction. J Biol Chem 262:10185-8
Mochly-Rosen, D; Koshland Jr, D E (1987) Domain structure and phosphorylation of protein kinase C. J Biol Chem 262:2291-7
Russo, A F; Koshland Jr, D E (1986) Identification of the tip-encoded receptor in bacterial sensing. J Bacteriol 165:276-82
Chelsky, D; Ruskin, B; Koshland Jr, D E (1985) Methyl-esterified proteins in a mammalian cell line. Biochemistry 24:6651-8
Stock, A; Koshland Jr, D E; Stock, J (1985) Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation. Proc Natl Acad Sci U S A 82:7989-93