Article
Phenotypically selected mutations in myosin's actin binding domain demonstrate intermolecular contacts important for motor function.
Biochemistry - 15 Jul 1997
Giese K C, Spudich J A
Abstract excerpt
Here, we biochemically characterize Dictyostelium myosin II mutants that were previously phenotypically selected following random mutagenesis and shown to lie in the actin binding domain [Patterson, B., & Spudich, J. A. (1996) Genetics 143, 801-810]. We show that the conditional loss of myosin-de...
Topics
- Actins
- Adenosine Triphosphate
- Animals
- Binding Sites
- Cloning, Molecular
- Dictyostelium
- Electrophoresis, Polyacrylamide Gel
- Enzyme Activation
- Gene Expression
- Kinetics
- Models, Molecular
- Mutagenesis
- Myosin Subfragments
- Myosins
- Phenotype
- Protein Conformation
- Spectrometry, Fluorescence