The long term goal is to solve the long-standing question of how myosin functions as a motor. The principal investigator proposes to determine the biochemical defect in the myosins from cold sensitive mutants in order to uncover which part of the mechanical cycle is perturbed. He will then isolate intragenic suppressor mutations to these cold- sensitive mutants and determine the sites of reversion. He will then characterize these suppressor strains, and select some for further biochemical characterization. Finally. he will characterize biochemical myosins carrying the suppressor mutations after separation from the original cold-sensitive mutations. The principal investigator plans to confirm, modify or replace models for the various conformations that myosin assumes during its mechanical cycle.
| Wu, Y; Nejad, M; Patterson, B (1999) Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release. Genetics 153:107-16 |
| Patterson, B (1998) Intragenic suppressors of Dictyostelium myosin G680 mutants demarcate discrete structural elements. Implications for conformational states of the motor. Genetics 149:1799-807 |
| Patterson, B; Ruppel, K M; Wu, Y et al. (1997) Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects. J Biol Chem 272:27612-7 |
