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.
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 |