This research is directed toward understanding biological assembly processes at the molecular level, using assembly of the bacteriophage lambda virion as a model. The research focuses on assembly processes in which one protein influences or directs the assembly of another, and seeks to understand the detailed mechanisms behind such events. Specific problems being addressed include the structure and regulation of the E. coli GroE proteins, which are host proteins required for correct virus assembly, the nature and role of protein processing during virus assembly, and the mechanisms by which the tail tape measure protein determines tail length.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI012227-13
Application #
3125142
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1977-12-01
Project End
1990-11-30
Budget Start
1986-12-01
Budget End
1987-11-30
Support Year
13
Fiscal Year
1987
Total Cost
Indirect Cost
Name
University of Pittsburgh
Department
Type
Schools of Arts and Sciences
DUNS #
053785812
City
Pittsburgh
State
PA
Country
United States
Zip Code
15213
Popa, M P; McKelvey, T A; Hempel, J et al. (1991) Bacteriophage HK97 structure: wholesale covalent cross-linking between the major head shell subunits. J Virol 65:3227-37
Hendrix, R W (1988) Tail length determination in double-stranded DNA bacteriophages. Curr Top Microbiol Immunol 136:21-9
Murphy, K C; Casey, L; Yannoutsos, N et al. (1987) Localization of a DNA-binding determinant in the bacteriophage P22 Erf protein. J Mol Biol 194:105-17
Chandrasekhar, G N; Tilly, K; Woolford, C et al. (1986) Purification and properties of the groES morphogenetic protein of Escherichia coli. J Biol Chem 261:12414-9
Cowing, D W; Bardwell, J C; Craig, E A et al. (1985) Consensus sequence for Escherichia coli heat shock gene promoters. Proc Natl Acad Sci U S A 82:2679-83