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-dependent activity in vivo, which results from the mutations E531Q, P536R, and R562L, is likely due to the loss of...
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